메뉴 건너뛰기




Volumn 5, Issue 18, 2008, Pages 15-45

Single-molecule biophysics: At the interface of biology, physics and chemistry

Author keywords

AFM; Force; FRET; Optical tweezers; Single molecule fluorescence; Tracking

Indexed keywords

DNA; RNA;

EID: 36348946234     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2007.1021     Document Type: Review
Times cited : (246)

References (323)
  • 1
    • 28544432440 scopus 로고    scopus 로고
    • Direct observation of base-pair stepping by RNA polymerase
    • doi:10.1038/nature04268
    • Abbondanzieri, E. A., Greenleaf, W. J., Shaevitz, J. W., Landick, R. & Block, S. M. 2005 Direct observation of base-pair stepping by RNA polymerase. Nature 438, 460-465. (doi:10.1038/nature04268)
    • (2005) Nature , vol.438 , pp. 460-465
    • Abbondanzieri, E.A.1    Greenleaf, W.J.2    Shaevitz, J.W.3    Landick, R.4    Block, S.M.5
  • 2
    • 0034690806 scopus 로고    scopus 로고
    • Stepping rotation of F-1-ATPase visualized through angle-resolved single-fluorophore imaging
    • doi:10.1073/pnas.120174297
    • Adachi, K., Yasuda, R., Noji, H., Itoh, H., Harada, Y., Yoshida, M. & Kinosita, K. 2000 Stepping rotation of F-1-ATPase visualized through angle-resolved single-fluorophore imaging. Proc. Natl Acad. Sci. USA 97, 7243-7247. (doi:10.1073/pnas.120174297)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7243-7247
    • Adachi, K.1    Yasuda, R.2    Noji, H.3    Itoh, H.4    Harada, Y.5    Yoshida, M.6    Kinosita, K.7
  • 3
    • 0030924943 scopus 로고    scopus 로고
    • Optical trapping and manipulation of neutral particles using lasers
    • doi:10.1073/pnas.94.10.4853
    • Ashkin, A. 1997 Optical trapping and manipulation of neutral particles using lasers. Proc. Natl Acad. Sci. USA 94, 4853-4860. (doi:10.1073/pnas.94.10.4853)
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4853-4860
    • Ashkin, A.1
  • 4
    • 0022655537 scopus 로고
    • Observation of a single-beam gradient force optical trap for dielectric particles
    • Ashkin, A., Dziedzic, J. M., Bjorkholm, J. E. & Chu, S. 1986 Observation of a single-beam gradient force optical trap for dielectric particles. Optics Lett. 11, 288-290.
    • (1986) Optics Lett , vol.11 , pp. 288-290
    • Ashkin, A.1    Dziedzic, J.M.2    Bjorkholm, J.E.3    Chu, S.4
  • 5
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • doi:10.1034/j.1600-0854.2001. 21104.x
    • Axelrod, D. 2001 Total internal reflection fluorescence microscopy in cell biology. Traffic 2, 764-774. (doi:10.1034/j.1600-0854.2001. 21104.x)
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 6
    • 33744925656 scopus 로고    scopus 로고
    • Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy: Theory and applications
    • doi:10.1529/biophysj.105. 075937
    • Barsegov, V., Klimov, D. K. & Thirumalai, D. 2006 Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy: theory and applications. Biophys. J. 90, 3827-3841. (doi:10.1529/biophysj.105. 075937)
    • (2006) Biophys. J , vol.90 , pp. 3827-3841
    • Barsegov, V.1    Klimov, D.K.2    Thirumalai, D.3
  • 7
    • 0242500997 scopus 로고    scopus 로고
    • Exploration of the transition state for tertiary structure formation between an RNA helix and a large structured RNA
    • doi:10.1016/S0022-2836(03)00272-9
    • Bartley, L. E., Zhuang, X. W., Das, R., Chu, S. & Herschlag, D. 2003 Exploration of the transition state for tertiary structure formation between an RNA helix and a large structured RNA. J. Mol. Biol. 328, 1011-1026. (doi:10.1016/S0022-2836(03)00272-9)
    • (2003) J. Mol. Biol , vol.328 , pp. 1011-1026
    • Bartley, L.E.1    Zhuang, X.W.2    Das, R.3    Chu, S.4    Herschlag, D.5
  • 8
    • 0004036109 scopus 로고    scopus 로고
    • Basche, T, Moerner, W. E, Orrit, M. & Wild, U. P, eds, Weinheim, Germany: VCH
    • Basche, T., Moerner, W. E., Orrit, M. & Wild, U. P. (eds) 1996 Single-molecule optical detection, imaging and spectroscopy. Weinheim, Germany: VCH.
    • (1996) Single-molecule optical detection, imaging and spectroscopy
  • 9
    • 33747067415 scopus 로고    scopus 로고
    • AFM imaging of protein movements: Histone H2A-H2B release during nucleosome remodeling
    • doi:10.1016/ j.febslet.2006.06.101
    • Bash, R., Wang, H., Anderson, C., Yodh, J., Hager, G., Lindsay, S. M. & Lohr, D. 2006 AFM imaging of protein movements: histone H2A-H2B release during nucleosome remodeling. FEBS Lett. 580, 4757-4761. (doi:10.1016/ j.febslet.2006.06.101)
    • (2006) FEBS Lett , vol.580 , pp. 4757-4761
    • Bash, R.1    Wang, H.2    Anderson, C.3    Yodh, J.4    Hager, G.5    Lindsay, S.M.6    Lohr, D.7
  • 10
    • 18044373456 scopus 로고    scopus 로고
    • Short-range spectroscopic ruler based on a single-molecule optical switch
    • doi:10.1103/Phys-RevLett.94.108101
    • Bates, M., Blosser, T. R. & Zhuang, X. 2005 Short-range spectroscopic ruler based on a single-molecule optical switch. Phys. Rev. Lett. 94, 108 101. (doi:10.1103/Phys-RevLett.94.108101)
    • (2005) Phys. Rev. Lett , vol.94 , pp. 108-101
    • Bates, M.1    Blosser, T.R.2    Zhuang, X.3
  • 11
    • 0345552211 scopus 로고    scopus 로고
    • Bennink, M. L., Scharer, O. D., Kanaar, R., Sakata-Sogawa, K., Schins, J. M., Kanger, J. S., de Grooth, B. G. & Greve, J. 1999 Single- moleculemanipulation of double-stranded DNA using optical tweezers: interaction studies of DNA with RecA and YOYO-1. Cytometry 36, 200-208. (doi:10.1002/ (SICI)1097-0320(19990701)36:3〈200::AID-CYTO9〉3.0. CO;2-T)
    • Bennink, M. L., Scharer, O. D., Kanaar, R., Sakata-Sogawa, K., Schins, J. M., Kanger, J. S., de Grooth, B. G. & Greve, J. 1999 Single- moleculemanipulation of double-stranded DNA using optical tweezers: interaction studies of DNA with RecA and YOYO-1. Cytometry 36, 200-208. (doi:10.1002/ (SICI)1097-0320(19990701)36:3〈200::AID-CYTO9〉3.0. CO;2-T)
  • 12
    • 0027768732 scopus 로고
    • Single molecules observed by near-field scanning optical microscopy
    • doi:10.1126/science.262.5138.1422
    • Betzig, E. & Chichester, R. J. 1993 Single molecules observed by near-field scanning optical microscopy. Science 262, 1422-1425. (doi:10.1126/science.262.5138.1422)
    • (1993) Science , vol.262 , pp. 1422-1425
    • Betzig, E.1    Chichester, R.J.2
  • 15
    • 0012618901 scopus 로고
    • Atomic force microscope
    • doi:10.1103/ PhysRevLett.56.930
    • Binnig, G., Quate, C. F. & Gerber, C. 1986 Atomic force microscope. Phys. Rev. Lett. 56, 930-933. (doi:10.1103/ PhysRevLett.56.930)
    • (1986) Phys. Rev. Lett , vol.56 , pp. 930-933
    • Binnig, G.1    Quate, C.F.2    Gerber, C.3
  • 18
    • 0030592549 scopus 로고    scopus 로고
    • Fifty ways to love your lever: Myosin motors
    • doi:10.1016/S0092-8674(00) 81332-X
    • Block, S. M. 1996 Fifty ways to love your lever: myosin motors. Cell 87, 151-157. (doi:10.1016/S0092-8674(00) 81332-X)
    • (1996) Cell , vol.87 , pp. 151-157
    • Block, S.M.1
  • 19
    • 34247571461 scopus 로고    scopus 로고
    • Kinesin motor mechanics: Binding, stepping, tracking, gating, and limping
    • doi:10.1529/biophysj.106.100677
    • Block, S. M. 2007 Kinesin motor mechanics: binding, stepping, tracking, gating, and limping. Biophys. J. 92, 2986-2995. (doi:10.1529/biophysj.106.100677)
    • (2007) Biophys. J , vol.92 , pp. 2986-2995
    • Block, S.M.1
  • 20
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • doi:10.1038/348348a0
    • Block, S. M., Goldstein, L. S. B. & Schnapp, B. J. 1990 Bead movement by single kinesin molecules studied with optical tweezers. Nature 348, 348-352. (doi:10.1038/348348a0)
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 21
    • 23744470902 scopus 로고    scopus 로고
    • Single-molecule RNA folding
    • doi:10.1021/ ar040142o
    • Bokinsky, G. & Zhuang, X. W. 2005 Single-molecule RNA folding. Acc. Chem. Res. 38, 566-573. (doi:10.1021/ ar040142o)
    • (2005) Acc. Chem. Res , vol.38 , pp. 566-573
    • Bokinsky, G.1    Zhuang, X.W.2
  • 22
    • 33746793263 scopus 로고    scopus 로고
    • Two distinct binding modes of a protein cofactor with its target RNA
    • doi:10.1016/j.jmb.2006.06.048
    • Bokinsky, G., Nivon, L. G., Liu, S. X., Chai, G. Q., Hong, M., Weeks, K. M. & Zhuang, X. W. 2006 Two distinct binding modes of a protein cofactor with its target RNA. J. Mol. Biol. 361, 771-784. (doi:10.1016/j.jmb.2006.06.048)
    • (2006) J. Mol. Biol , vol.361 , pp. 771-784
    • Bokinsky, G.1    Nivon, L.G.2    Liu, S.X.3    Chai, G.Q.4    Hong, M.5    Weeks, K.M.6    Zhuang, X.W.7
  • 23
    • 33845669025 scopus 로고    scopus 로고
    • Many expressed genes in bacteria and yeast are transcribed only once per cell cycle
    • doi:10.1096/fj.06-6087fje
    • Bon, M., McGowan, S. J.& Cook, P. R. 2006 Many expressed genes in bacteria and yeast are transcribed only once per cell cycle. FASEB J. 20, 1721-1723. (doi:10.1096/fj.06-6087fje)
    • (2006) FASEB J , vol.20 , pp. 1721-1723
    • Bon, M.1    McGowan, S.J.2    Cook, P.R.3
  • 24
    • 0032555119 scopus 로고    scopus 로고
    • Kinetics of conformational fluctuations in DNA hairpin-loops
    • doi:10.1073/pnas.95. 15.8602
    • Bonnet, G., Krichevsky, O. & Libchaber, A. 1998 Kinetics of conformational fluctuations in DNA hairpin-loops. Proc. Natl Acad. Sci. USA 95, 8602-8606. (doi:10.1073/pnas.95. 15.8602)
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8602-8606
    • Bonnet, G.1    Krichevsky, O.2    Libchaber, A.3
  • 25
    • 23844545227 scopus 로고    scopus 로고
    • Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer
    • doi:10.1042/ BST0330878
    • Borsch, M. & Graber, P. 2005 Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer. Biochem. Soc. Trans. 33, 878-882. (doi:10.1042/ BST0330878)
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 878-882
    • Borsch, M.1    Graber, P.2
  • 26
    • 0037063327 scopus 로고    scopus 로고
    • Stepwise rotation of the gamma-subunit of EF0F1-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer
    • doi:10.1016/S0014-5793(02)03198-8
    • Borsch, M., Diez, M., Zimmermann, B., Reuter, R. & Graber, P. 2002 Stepwise rotation of the gamma-subunit of EF0F1-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer. FEBS Lett. 527, 147-152. (doi:10.1016/S0014-5793(02)03198-8)
    • (2002) FEBS Lett , vol.527 , pp. 147-152
    • Borsch, M.1    Diez, M.2    Zimmermann, B.3    Reuter, R.4    Graber, P.5
  • 27
    • 23144455040 scopus 로고    scopus 로고
    • Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex
    • doi:10.1529/biophysj.104. 054064
    • Bowen, M. E., Weninger, K., Ernst, J., Chu, S. & Brunger, A. T. 2005 Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophys. J. 89, 690-702. (doi:10.1529/biophysj.104. 054064)
    • (2005) Biophys. J , vol.89 , pp. 690-702
    • Bowen, M.E.1    Weninger, K.2    Ernst, J.3    Chu, S.4    Brunger, A.T.5
  • 29
    • 0037133348 scopus 로고    scopus 로고
    • Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA
    • doi:10.1073/pnas.022638399
    • Brower-Toland, B. D., Smith, C. L., Yeh, R. C., Lis, J. T., Peterson, C. L. & Wang, M. D. 2002 Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA. Proc. Natl Acad. Sci. USA 99, 1960-1965. (doi:10.1073/pnas.022638399)
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1960-1965
    • Brower-Toland, B.D.1    Smith, C.L.2    Yeh, R.C.3    Lis, J.T.4    Peterson, C.L.5    Wang, M.D.6
  • 30
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • doi:10.1038/nphys269
    • Brujic, J., Hermans, R. I., Walther, K. A. & Fernandez, J. M. 2006 Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin. Nat. Phys. 2, 282-286. (doi:10.1038/nphys269)
    • (2006) Nat. Phys , vol.2 , pp. 282-286
    • Brujic, J.1    Hermans, R.I.2    Walther, K.A.3    Fernandez, J.M.4
  • 31
    • 0023449962 scopus 로고
    • Spin-glasses and the statistical-mechanics of protein folding
    • doi:10.1073/pnas.84.21.7524
    • Bryngelson, J. D. & Wolynes, P. G. 1987 Spin-glasses and the statistical-mechanics of protein folding. Proc. Natl Acad. Sci. USA 84, 7524-7528. (doi:10.1073/pnas.84.21.7524)
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 32
    • 0028947257 scopus 로고
    • Funnels pathways, and the energy landscape of protein-folding - a synthesis
    • doi:10.1002/prot. 340210302
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D. & Wolynes, P. G. 1995 Funnels pathways, and the energy landscape of protein-folding - a synthesis. Proteins - Struct. Funct. Genet. 21, 167-195. (doi:10.1002/prot. 340210302)
    • (1995) Proteins - Struct. Funct. Genet , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 33
    • 0034328878 scopus 로고    scopus 로고
    • Grabbing the cat by the tail: Manipulating molecules one by one
    • doi:10.1038/35040072
    • Bustamante, C., Macosko, J. C. & Wuite, G. J. L. 2000 Grabbing the cat by the tail: manipulating molecules one by one. Nat. Rev. Mol. Cell Biol. 1, 130-136. (doi:10.1038/35040072)
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , pp. 130-136
    • Bustamante, C.1    Macosko, J.C.2    Wuite, G.J.L.3
  • 34
    • 3943069115 scopus 로고    scopus 로고
    • Mechanical processes in biochemistry
    • doi:10.1146/annurev.biochem.72. 121801.161542
    • Bustamante, C., Chemla, Y. R., Forde, N. R. & Izhaky, D. 2004 Mechanical processes in biochemistry. Annu. Rev. Biochem. 73, 705-748. (doi:10.1146/annurev.biochem.72. 121801.161542)
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 705-748
    • Bustamante, C.1    Chemla, Y.R.2    Forde, N.R.3    Izhaky, D.4
  • 35
    • 23844508956 scopus 로고    scopus 로고
    • The nonequilibrium thermodynamics of small systems
    • doi:10.1063/1.2012462
    • Bustamante, C., Liphardt, J. & Ritort, F. 2005 The nonequilibrium thermodynamics of small systems. Phys. Today 58, 43-48. (doi:10.1063/1.2012462)
    • (2005) Phys. Today , vol.58 , pp. 43-48
    • Bustamante, C.1    Liphardt, J.2    Ritort, F.3
  • 37
    • 30844467976 scopus 로고    scopus 로고
    • Kinesin's moonwalk
    • doi:10.1016/j.ceb.2005.12.009
    • Carter, N. J. & Cross, R. A. 2006 Kinesin's moonwalk. Curr. Opin. Cell Biol. 18, 61-67. (doi:10.1016/j.ceb.2005.12.009)
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 61-67
    • Carter, N.J.1    Cross, R.A.2
  • 38
    • 33847281331 scopus 로고    scopus 로고
    • Stabilization of an optical microscope to 0.1 nm in three dimensions
    • doi:10.1364/AO.46. 000421
    • Carter, A. R., King, G. M., Ulrich, T. A., Halsey, W., Alchenberger, D. & Perkins, T. T. 2007 Stabilization of an optical microscope to 0.1 nm in three dimensions. Appl. Opt. 46, 421-427. (doi:10.1364/AO.46. 000421)
    • (2007) Appl. Opt , vol.46 , pp. 421-427
    • Carter, A.R.1    King, G.M.2    Ulrich, T.A.3    Halsey, W.4    Alchenberger, D.5    Perkins, T.T.6
  • 39
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • doi:10.1126/science.1116702
    • Cecconi, C., Shank, E. A., Bustamante, C. & Marqusee, S. 2005 Direct observation of the three-state folding of a single protein molecule. Science 309, 2057-2060. (doi:10.1126/science.1116702)
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 40
    • 33845186032 scopus 로고    scopus 로고
    • Femtosecond diffractive imaging with a soft-X-ray free-electron laser
    • doi:10.1038/nphys461
    • Chapman, H. N. et al. 2006 Femtosecond diffractive imaging with a soft-X-ray free-electron laser. Nat. Phys. 2, 839-843. (doi:10.1038/nphys461)
    • (2006) Nat. Phys , vol.2 , pp. 839-843
    • Chapman, H.N.1
  • 41
    • 0037195077 scopus 로고    scopus 로고
    • Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy
    • doi:10.1073/pnas.172524899
    • Chattopadhyay, K., Saffarian, S., Elson, E. L. & Frieden, C. 2002 Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 99, 14 171-14 176. (doi:10.1073/pnas.172524899)
    • (2002) Proc. Natl Acad. Sci. USA , vol.99
    • Chattopadhyay, K.1    Saffarian, S.2    Elson, E.L.3    Frieden, C.4
  • 42
    • 14044264279 scopus 로고    scopus 로고
    • The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods
    • doi:10.1073/pnas. 0500127102
    • Chattopadhyay, K., Elson, E. L. & Frieden, C. 2005 The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods. Proc. Natl Acad. Sci. USA 102, 2385-2389. (doi:10.1073/pnas. 0500127102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2385-2389
    • Chattopadhyay, K.1    Elson, E.L.2    Frieden, C.3
  • 43
    • 0034817343 scopus 로고    scopus 로고
    • Quantitative comparison of algorithms for tracking single fluorescent particles
    • Cheezum, M. K., Walker, W. F. & Guilford, W. H. 2001 Quantitative comparison of algorithms for tracking single fluorescent particles. Biophys. J. 81, 2378-2388.
    • (2001) Biophys. J , vol.81 , pp. 2378-2388
    • Cheezum, M.K.1    Walker, W.F.2    Guilford, W.H.3
  • 44
    • 24144478521 scopus 로고    scopus 로고
    • Mechanism of force generation of a viral DNA packaging motor
    • doi:10.1016/j.cell. 2005.06.024
    • Chemla, Y. R., Aathavan, K., Michaelis, J., Grimes, S., Jardine, P. J., Anderson, D. L. & Bustamante, C. 2005 Mechanism of force generation of a viral DNA packaging motor. Cell 122, 683-692. (doi:10.1016/j.cell. 2005.06.024)
    • (2005) Cell , vol.122 , pp. 683-692
    • Chemla, Y.R.1    Aathavan, K.2    Michaelis, J.3    Grimes, S.4    Jardine, P.J.5    Anderson, D.L.6    Bustamante, C.7
  • 45
    • 13844276672 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with small molecules in live cells
    • doi:10.1016/j.copbio.2004.12.003
    • Chen, I. & Ting, A. Y. 2005 Site-specific labeling of proteins with small molecules in live cells. Curr. Opin. Biotechnol. 16, 35-40. (doi:10.1016/j.copbio.2004.12.003)
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 35-40
    • Chen, I.1    Ting, A.Y.2
  • 46
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Chen, Y., Muller, J. D., So, P. T. & Gratton, E. 1999 The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys. J. 77, 553-567.
    • (1999) Biophys. J , vol.77 , pp. 553-567
    • Chen, Y.1    Muller, J.D.2    So, P.T.3    Gratton, E.4
  • 47
    • 22944437806 scopus 로고    scopus 로고
    • Massively parallel manipulation of single cells and microparticles using optical images
    • doi:10.1038/ nature03831
    • Chiou, P. Y., Ohta, A. T. & Wu, M. C. 2005 Massively parallel manipulation of single cells and microparticles using optical images. Nature 436, 370-372. (doi:10.1038/ nature03831)
    • (2005) Nature , vol.436 , pp. 370-372
    • Chiou, P.Y.1    Ohta, A.T.2    Wu, M.C.3
  • 48
    • 33646591544 scopus 로고    scopus 로고
    • Transcriptional pulsing of a developmental gene
    • doi:10.1016/j.cub.2006.03.092
    • Chubb, J. R., Trcek, T., Shenoy, S. M. & Singer, R. H. 2006 Transcriptional pulsing of a developmental gene. Curr. Biol. 16, 1018-1025. (doi:10.1016/j.cub.2006.03.092)
    • (2006) Curr. Biol , vol.16 , pp. 1018-1025
    • Chubb, J.R.1    Trcek, T.2    Shenoy, S.M.3    Singer, R.H.4
  • 49
    • 13444291091 scopus 로고    scopus 로고
    • Three-color single-molecule fluorescence resonance energy transfer
    • doi:10.1002/cphc.200400261
    • Clamme, J. P. & Deniz, A. A. 2005 Three-color single-molecule fluorescence resonance energy transfer. Chemphyschem 6, 74-77. (doi:10.1002/cphc.200400261)
    • (2005) Chemphyschem , vol.6 , pp. 74-77
    • Clamme, J.P.1    Deniz, A.A.2
  • 50
    • 0033781080 scopus 로고    scopus 로고
    • Force spectroscopy with single bio-molecules
    • doi:10.1016/S1367-5931(00)00126-5
    • Clausen-Schaumann, H., Seitz, M., Krautbauer, R. & Gaub, H. E. 2000 Force spectroscopy with single bio-molecules. Curr. Opin. Chem. Biol. 4, 524-530. (doi:10.1016/S1367-5931(00)00126-5)
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 524-530
    • Clausen-Schaumann, H.1    Seitz, M.2    Krautbauer, R.3    Gaub, H.E.4
  • 52
    • 33645223271 scopus 로고    scopus 로고
    • Suppressing Brownian motion of individual biomolecules in solution
    • doi:10.1073/pnas. 0509976103
    • Cohen, A. E. & Moerner, W. E. 2006 Suppressing Brownian motion of individual biomolecules in solution. Proc. Natl Acad. Sci. USA 103, 4362-4365. (doi:10.1073/pnas. 0509976103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4362-4365
    • Cohen, A.E.1    Moerner, W.E.2
  • 53
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • doi:10.1371/journal.pbio.0020321
    • Collins, S. R., Douglass, A., Vale, R. D. & Weissman, J. S. 2004 Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2, 1582-1590. (doi:10.1371/journal.pbio.0020321)
    • (2004) PLoS Biol , vol.2 , pp. 1582-1590
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 54
    • 24644450199 scopus 로고    scopus 로고
    • Verification of the Crooks fluctuation theorem and recovery of RNA folding free energies
    • doi:10.1038/nature04061
    • Collin, D., Ritort, F., Jarzynski, C., Smith, S. B., Tinoco, I. & Bustamante, C. 2005 Verification of the Crooks fluctuation theorem and recovery of RNA folding free energies. Nature 437, 231-234. (doi:10.1038/nature04061)
    • (2005) Nature , vol.437 , pp. 231-234
    • Collin, D.1    Ritort, F.2    Jarzynski, C.3    Smith, S.B.4    Tinoco, I.5    Bustamante, C.6
  • 55
    • 0030003076 scopus 로고    scopus 로고
    • Studies on single alkaline phosphatase molecules: Reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation - the death of an enzyme
    • doi:10.1021/ja9540839
    • Craig, D. B., Arriaga, E. A., Wong, J. C. Y., Lu, H. & Dovichi, N. J. 1996 Studies on single alkaline phosphatase molecules: reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation - the death of an enzyme. J. Am. Chem. Soc. 118, 5245-5253. (doi:10.1021/ja9540839)
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 5245-5253
    • Craig, D.B.1    Arriaga, E.A.2    Wong, J.C.Y.3    Lu, H.4    Dovichi, N.J.5
  • 57
    • 0034711368 scopus 로고    scopus 로고
    • Nanoelectromechanical systems
    • doi:10.1126/science.290.5496. 1532
    • Craighead, H. G. 2000 Nanoelectromechanical systems. Science 290, 1532-1536. (doi:10.1126/science.290.5496. 1532)
    • (2000) Science , vol.290 , pp. 1532-1536
    • Craighead, H.G.1
  • 58
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • doi:10.1126/science.1088525
    • Dahan, M., Levi, S., Luccardini, C., Rostaing, P., Riveau, B. & Triller, A. 2003 Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302, 442-445. (doi:10.1126/science.1088525)
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Levi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 60
    • 4143135445 scopus 로고    scopus 로고
    • Single-molecule study of RuvAB-mediated Holliday-junction migration
    • doi:10.1073/pnas.0404369101
    • Dawid, A., Croquette, V., Grigoriev, M. & Heslot, F. 2004 Single-molecule study of RuvAB-mediated Holliday-junction migration. Proc. Natl Acad. Sci. USA 101, 11 611-11 616. (doi:10.1073/pnas.0404369101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101
    • Dawid, A.1    Croquette, V.2    Grigoriev, M.3    Heslot, F.4
  • 61
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • doi:10.1146/annurev.biochem.69.1.923
    • Dawson, P. E. & Kent, S. B. H. 2000 Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69, 923-960. (doi:10.1146/annurev.biochem.69.1.923)
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.H.2
  • 62
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Forster distance dependence and subpopulations
    • doi:10.1073/pnas.96.7.3670
    • Deniz, A. A., Dahan, M., Grunwell, J. R., Ha, T., Faulhaber, A. E., Chemla, D. S., Weiss, S. & Schultz, P. G. 1999 Single-pair fluorescence resonance energy transfer on freely diffusing molecules: observation of Forster distance dependence and subpopulations. Proc. Natl Acad. Sci. USA 96, 3670-3675. (doi:10.1073/pnas.96.7.3670)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 63
    • 0034625167 scopus 로고    scopus 로고
    • Single-molecule protein folding: Diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2
    • doi:10.1073/pnas. 090104997
    • Deniz, A. A., Laurence, T. A., Beligere, G. S., Dahan, M., Martin, A. B., Chemla, D. S., Dawson, P. E., Schultz, P. G. & Weiss, S. 2000 Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. Proc. Natl Acad. Sci. USA 97, 5179-5184. (doi:10.1073/pnas. 090104997)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5179-5184
    • Deniz, A.A.1    Laurence, T.A.2    Beligere, G.S.3    Dahan, M.4    Martin, A.B.5    Chemla, D.S.6    Dawson, P.E.7    Schultz, P.G.8    Weiss, S.9
  • 64
    • 0034743156 scopus 로고    scopus 로고
    • Ratiometric single-molecule studies of freely diffusing biomolecules
    • doi:10.1146/annurev. physchem.52.1.233
    • Deniz, A. A., Laurence, T. A., Dahan, M., Chemla, D. S., Schultz, P. G. & Weiss, S. 2001 Ratiometric single-molecule studies of freely diffusing biomolecules. Annu. Rev. Phys. Chem. 52, 233-253. (doi:10.1146/annurev. physchem.52.1.233)
    • (2001) Annu. Rev. Phys. Chem , vol.52 , pp. 233-253
    • Deniz, A.A.1    Laurence, T.A.2    Dahan, M.3    Chemla, D.S.4    Schultz, P.G.5    Weiss, S.6
  • 65
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • doi:10.1126/science.2321027
    • Denk, W., Strickler, J. H. & Webb, W. W. 1990 Two-photon laser scanning fluorescence microscopy. Science 248, 73-76. (doi:10.1126/science.2321027)
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 66
    • 0030575902 scopus 로고    scopus 로고
    • Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels
    • doi:10.1126/science. 274.5289.966
    • Dickson, R. M., Norris, D. J., Tzeng, Y. L. & Moerner, W. E. 1996 Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels. Science 274, 966-969. (doi:10.1126/science. 274.5289.966)
    • (1996) Science , vol.274 , pp. 966-969
    • Dickson, R.M.1    Norris, D.J.2    Tzeng, Y.L.3    Moerner, W.E.4
  • 67
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • doi:10.1038/ nsb0197-10
    • Dill, K. A. & Chan, H. S. 1997 From Levinthal to pathways to funnels. Nat. Struct. Biol. 4, 10-19. (doi:10.1038/ nsb0197-10)
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 68
    • 33845191735 scopus 로고    scopus 로고
    • Nucleophilic catalysis of oxime ligation
    • doi:10.1002/anie.200602877
    • Dirksen, A., Hackeng, T. M. & Dawson, P. E. 2006 Nucleophilic catalysis of oxime ligation. Angew. Chem. Int. Edn. 45, 7581-7584. (doi:10.1002/anie.200602877)
    • (2006) Angew. Chem. Int. Edn , vol.45 , pp. 7581-7584
    • Dirksen, A.1    Hackeng, T.M.2    Dawson, P.E.3
  • 69
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • doi:10.1016/j.cell.2005.04.009
    • Douglass, A. D. & Vale, R. D. 2005 Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121, 937-950. (doi:10.1016/j.cell.2005.04.009)
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 70
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • doi:10.1103/ PhysRevLett.96.108101
    • Dudko, O. K., Hummer, G. & Szabo, A. 2006 Intrinsic rates and activation free energies from single-molecule pulling experiments. Phys. Rev. Lett. 96, 108 101. (doi:10.1103/ PhysRevLett.96.108101)
    • (2006) Phys. Rev. Lett , vol.96 , pp. 108-101
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 71
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCVNS3 helicase and its coordination by ATP
    • doi:10.1038/ nature04331
    • Dumont, S., Cheng, W., Serebrov, V., Beran, R. K., Tinoco, I., Pyle, A. M. & Bustamante, C. 2006 RNA translocation and unwinding mechanism of HCVNS3 helicase and its coordination by ATP. Nature 439, 105-108. (doi:10.1038/ nature04331)
    • (2006) Nature , vol.439 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco, I.5    Pyle, A.M.6    Bustamante, C.7
  • 72
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • doi:10.1146/annurev.biophys.32.110601. 142439
    • Edidin, M. 2003 The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32, 257-283. (doi:10.1146/annurev.biophys.32.110601. 142439)
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 73
    • 0034682520 scopus 로고    scopus 로고
    • Memory landscapes of singleenzyme molecules
    • doi:10.1073/pnas.130589397
    • Edman, L. & Rigler, R. 2000 Memory landscapes of singleenzyme molecules. Proc. Natl Acad. Sci. USA 97, 8266-8271. (doi:10.1073/pnas.130589397)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8266-8271
    • Edman, L.1    Rigler, R.2
  • 74
    • 33645678319 scopus 로고    scopus 로고
    • Analysis of photo-bleaching in single-molecule multicolor excitation and forster resonance energy transfer measurement
    • doi:10.1021/jp054581w
    • Eggeling, C., Widengren, J., Brand, L., Schaffer, J., Felekyan, S. & Seidel, C. A. M. 2006 Analysis of photo-bleaching in single-molecule multicolor excitation and forster resonance energy transfer measurement. J. Phys. Chem. A 110, 2979-2995. (doi:10.1021/jp054581w)
    • (2006) J. Phys. Chem. A , vol.110 , pp. 2979-2995
    • Eggeling, C.1    Widengren, J.2    Brand, L.3    Schaffer, J.4    Felekyan, S.5    Seidel, C.A.M.6
  • 75
    • 16844363110 scopus 로고    scopus 로고
    • Fluorescence microscopy with super-resolved optical sections
    • doi:10.1016/j.tcb.2005.02.003
    • Egner, A. & Hell, S. W. 2005 Fluorescence microscopy with super-resolved optical sections. Trends Cell Biol. 15, 207-215. (doi:10.1016/j.tcb.2005.02.003)
    • (2005) Trends Cell Biol , vol.15 , pp. 207-215
    • Egner, A.1    Hell, S.W.2
  • 76
    • 0028229903 scopus 로고
    • Sorting single molecules - application to diagnostics and evolutionary biotechnology
    • doi:10.1073/ pnas.91.13.5740
    • Eigen, M. & Rigler, R. 1994 Sorting single molecules - application to diagnostics and evolutionary biotechnology. Proc. Natl Acad. Sci. USA 91, 5740-5747. (doi:10.1073/ pnas.91.13.5740)
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 77
    • 0025855016 scopus 로고
    • Biological applications of scanning probe microscopes
    • doi:10.1146/annurev.bb.20.060191.000455
    • Engel, A. 1991 Biological applications of scanning probe microscopes. Annu. Rev. Biophys. Biophys. Chem. 20, 79-108. (doi:10.1146/annurev.bb.20.060191.000455)
    • (1991) Annu. Rev. Biophys. Biophys. Chem , vol.20 , pp. 79-108
    • Engel, A.1
  • 78
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • doi:10.1038/78929
    • Engel, A. & Muller, D. J. 2000 Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7, 715-718. (doi:10.1038/78929)
    • (2000) Nat. Struct. Biol , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 79
    • 0032562720 scopus 로고    scopus 로고
    • Visualization of single RNA transcripts in situ
    • doi:10.1126/science.280.5363.585
    • Femino, A., Fay, F. S., Fogarty, K. & Singer, R. H. 1998 Visualization of single RNA transcripts in situ. Science 280, 585-590. (doi:10.1126/science.280.5363.585)
    • (1998) Science , vol.280 , pp. 585-590
    • Femino, A.1    Fay, F.S.2    Fogarty, K.3    Singer, R.H.4
  • 80
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • doi:10.1126/science.1092497
    • Fernandez, J. M. & Li, H. 2004 Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303, 1674-1678. (doi:10.1126/science.1092497)
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 81
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • doi:10.1038/78936
    • Fisher, T. E., Marszalek, P. E. & Fernandez, J. M. 2000 Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7, 719-724. (doi:10.1038/78936)
    • (2000) Nat. Struct. Biol , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 82
    • 33744802398 scopus 로고    scopus 로고
    • Effects of surface tethering on protein folding mechanisms
    • doi:10.1073/pnas. 0601210103
    • Friedel, M., Baumketner, A. & Shea, J. E. 2006 Effects of surface tethering on protein folding mechanisms. Proc. Natl Acad. Sci. USA 103, 8396-8401. (doi:10.1073/pnas. 0601210103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8396-8401
    • Friedel, M.1    Baumketner, A.2    Shea, J.E.3
  • 83
    • 0036400525 scopus 로고    scopus 로고
    • What fluorescence correlation spectroscopy can tell us about unfolded proteins
    • Frieden, C., Chattopadhyay, K. & Elson, E. L. 2002 What fluorescence correlation spectroscopy can tell us about unfolded proteins. Unfolded Proteins 62, 91-109.
    • (2002) Unfolded Proteins , vol.62 , pp. 91-109
    • Frieden, C.1    Chattopadhyay, K.2    Elson, E.L.3
  • 84
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous-solution
    • doi:10.1038/ 374555a0
    • Funatsu, T., Harada, Y., Tokunaga, M., Saito, K. & Yanagida, T. 1995 Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous-solution. Nature 374, 555-559. (doi:10.1038/ 374555a0)
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 85
    • 0347156907 scopus 로고    scopus 로고
    • Single mRNA molecules demonstrate probabilistic movement in living mammalian cells
    • doi:10.1016/S0960-9822(02)01436-7
    • Fusco, D., Accornero, N., Lavoie, B., Shenoy, S. M., Blanchard, J. M., Singer, R. H. & Bertrand, E. 2003 Single mRNA molecules demonstrate probabilistic movement in living mammalian cells. Curr. Biol. 13, 161-167. (doi:10.1016/S0960-9822(02)01436-7)
    • (2003) Curr. Biol , vol.13 , pp. 161-167
    • Fusco, D.1    Accornero, N.2    Lavoie, B.3    Shenoy, S.M.4    Blanchard, J.M.5    Singer, R.H.6    Bertrand, E.7
  • 86
    • 22044436367 scopus 로고    scopus 로고
    • Forced unraveling of nucleosomes assembled on heterogeneous DNA using core, histones, NAP-1, and ACF
    • doi:10.1016/j.jmb.2005.05.058
    • Gemmen, G. J., Sim, R., Haushalter, K. A., Ke, P. C., Kadonaga, J. T. & Smith, D. E. 2005 Forced unraveling of nucleosomes assembled on heterogeneous DNA using core, histones, NAP-1, and ACF. J. Mol. Biol. 351, 89-99. (doi:10.1016/j.jmb.2005.05.058)
    • (2005) J. Mol. Biol , vol.351 , pp. 89-99
    • Gemmen, G.J.1    Sim, R.2    Haushalter, K.A.3    Ke, P.C.4    Kadonaga, J.T.5    Smith, D.E.6
  • 87
    • 18844445064 scopus 로고    scopus 로고
    • Sizing-up finite fluorescent particles with nanometer-scale precision by convolution and correlation image analysis
    • doi:10.1007/s00249-004- 0441-0
    • Gennerich, A. & Schild, D. 2005 Sizing-up finite fluorescent particles with nanometer-scale precision by convolution and correlation image analysis. Eur. Biophys. J. 34, 181-199. (doi:10.1007/s00249-004- 0441-0)
    • (2005) Eur. Biophys. J , vol.34 , pp. 181-199
    • Gennerich, A.1    Schild, D.2
  • 89
    • 33747880302 scopus 로고    scopus 로고
    • N-terminal protein modification through a biomimetic transamination reaction
    • doi:10.1002/anie. 200600368
    • Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S. & Francis, M. B. 2006 N-terminal protein modification through a biomimetic transamination reaction. Angew. Chem. Int. Edn. 45, 5307-5311. (doi:10.1002/anie. 200600368)
    • (2006) Angew. Chem. Int. Edn , vol.45 , pp. 5307-5311
    • Gilmore, J.M.1    Scheck, R.A.2    Esser-Kahn, A.P.3    Joshi, N.S.4    Francis, M.B.5
  • 90
    • 28944434119 scopus 로고    scopus 로고
    • Real-time kinetics of gene activity in individual bacteria
    • doi:10.1016/j.cell.2005.09.031
    • Golding, I., Paulsson, J., Zawilski, S. M. & Cox, E. C. 2005 Real-time kinetics of gene activity in individual bacteria. Cell 123, 1025-1036. (doi:10.1016/j.cell.2005.09.031)
    • (2005) Cell , vol.123 , pp. 1025-1036
    • Golding, I.1    Paulsson, J.2    Zawilski, S.M.3    Cox, E.C.4
  • 91
    • 0037566231 scopus 로고    scopus 로고
    • Single-macromolecule fluorescence resonance energy transfer and free-energy profiles
    • doi:10.1021/ jp027481o
    • Gopich, I. V. & Szabo, A. 2003 Single-macromolecule fluorescence resonance energy transfer and free-energy profiles. J. Phys. Chem. B 107, 5058-5063. (doi:10.1021/ jp027481o)
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5058-5063
    • Gopich, I.V.1    Szabo, A.2
  • 92
    • 34548096938 scopus 로고    scopus 로고
    • Theory of photon statistics in single-molecule Forster resonance energy transfer
    • doi:10.1063/1.1812746
    • Gopich, I. & Szabo, A. 2005 Theory of photon statistics in single-molecule Forster resonance energy transfer. J. Chem. Phys. 122, 014 707. (doi:10.1063/1.1812746)
    • (2005) J. Chem. Phys , vol.122 , pp. 014-707
    • Gopich, I.1    Szabo, A.2
  • 93
    • 2342582682 scopus 로고    scopus 로고
    • Single-molecule high-resolution imaging with photobleaching
    • doi:10.1073/pnas. 0401638101
    • Gordon, M. P., Ha, T. & Selvin, P. R. 2004 Single-molecule high-resolution imaging with photobleaching. Proc. Natl Acad. Sci. USA 101, 6462-6465. (doi:10.1073/pnas. 0401638101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6462-6465
    • Gordon, M.P.1    Ha, T.2    Selvin, P.R.3
  • 95
    • 0036111913 scopus 로고    scopus 로고
    • Magnetic tweezers: Micromanipulation and force measurement at the molecular level
    • Gosse, C. & Croquette, V. 2002 Magnetic tweezers: micromanipulation and force measurement at the molecular level. Biophys. J. 82, 3314-3329.
    • (2002) Biophys. J , vol.82 , pp. 3314-3329
    • Gosse, C.1    Croquette, V.2
  • 96
    • 33747103461 scopus 로고    scopus 로고
    • Single-molecule, motion-based DNA sequencing using RNA polymerase
    • doi:10.1126/science.1130105
    • Greenleaf, W. J. & Block, S. M. 2006 Single-molecule, motion-based DNA sequencing using RNA polymerase. Science 313, 801. (doi:10.1126/science.1130105)
    • (2006) Science , vol.313 , pp. 801
    • Greenleaf, W.J.1    Block, S.M.2
  • 97
    • 28844460238 scopus 로고    scopus 로고
    • Passive all-optical force clamp for high-resolution laser trapping
    • doi:10.1103/PhysRevLett.95.208102
    • Greenleaf, W. J., Woodside, M. T., Abbondanzieri, E. A. & Block, S. M. 2005 Passive all-optical force clamp for high-resolution laser trapping. Phys. Rev. Lett. 95, 208 102. (doi:10.1103/PhysRevLett.95.208102)
    • (2005) Phys. Rev. Lett , vol.95 , pp. 208-102
    • Greenleaf, W.J.1    Woodside, M.T.2    Abbondanzieri, E.A.3    Block, S.M.4
  • 98
    • 0041967046 scopus 로고    scopus 로고
    • A revolution in optical manipulation
    • doi:10.1038/nature01935
    • Grier, D. G. 2003 A revolution in optical manipulation. Nature 424, 810-816. (doi:10.1038/nature01935)
    • (2003) Nature , vol.424 , pp. 810-816
    • Grier, D.G.1
  • 99
    • 0029394767 scopus 로고
    • Does replication-induced transcription regulate synthesis of the myriad low copy number proteins of Escherichia coli?
    • doi:10.1002/ bies.950171112
    • Guptasarma, P. 1995 Does replication-induced transcription regulate synthesis of the myriad low copy number proteins of Escherichia coli? Bioessays 17, 987-997. (doi:10.1002/ bies.950171112)
    • (1995) Bioessays , vol.17 , pp. 987-997
    • Guptasarma, P.1
  • 100
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • doi:10.1073/ pnas.93.13.6264
    • Ha, T., Enderle, T., Ogletree, D. F., Chemla, D. S., Selvin, P. R. & Weiss, S. 1996 Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA 93, 6264-6268. (doi:10.1073/ pnas.93.13.6264)
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Ogletree, D.F.3    Chemla, D.S.4    Selvin, P.R.5    Weiss, S.6
  • 101
    • 0033529972 scopus 로고    scopus 로고
    • Ligand-induced conformational changes observed in single RNA molecules
    • doi:10.1073/pnas.96.16. 9077
    • Ha, T., Zhuang, X. W., Kim, H. D., Orr, J. W., Williamson, J. R.&Chu, S. 1999 Ligand-induced conformational changes observed in single RNA molecules. Proc. Natl Acad. Sci. USA 96, 9077-9082. (doi:10.1073/pnas.96.16. 9077)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9077-9082
    • Ha, T.1    Zhuang, X.W.2    Kim, H.D.3    Orr, J.W.4    Williamson, J.R.5    Chu, S.6
  • 102
    • 0033783987 scopus 로고    scopus 로고
    • Single-molecule X-ray diffraction
    • doi:10.1016/S0959-440X (00)00133-0
    • Hajdu, J. 2000 Single-molecule X-ray diffraction. Curr. Opin. Struct. Biol. 10, 569-573. (doi:10.1016/S0959-440X (00)00133-0)
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 569-573
    • Hajdu, J.1
  • 103
    • 0041140162 scopus 로고
    • The question of correlation between photons in coherent light rays
    • doi:10.1038/1781447a0
    • Hanbury Brown, R. & Twiss, R. Q. 1956 The question of correlation between photons in coherent light rays. Nature 178, 1447-1448. (doi:10.1038/1781447a0)
    • (1956) Nature , vol.178 , pp. 1447-1448
    • Hanbury Brown, R.1    Twiss, R.Q.2
  • 104
    • 33644770402 scopus 로고    scopus 로고
    • Measuring single molecule conductance with break junctions
    • doi:10.1039/ b508434m
    • He, J., Sankey, O., Lee, M., Tao, N. J., Li, X. L. & Lindsay, S. 2006 Measuring single molecule conductance with break junctions. Farad. Discuss. 131, 145-154. (doi:10.1039/ b508434m)
    • (2006) Farad. Discuss , vol.131 , pp. 145-154
    • He, J.1    Sankey, O.2    Lee, M.3    Tao, N.J.4    Li, X.L.5    Lindsay, S.6
  • 105
    • 0033621088 scopus 로고    scopus 로고
    • Polymerization and mechanical properties of single RecA-DNA filaments
    • doi:10.1073/pnas.96.18.10109
    • Hegner, M., Smith, S. B. & Bustamante, C. 1999 Polymerization and mechanical properties of single RecA-DNA filaments. Proc. Natl Acad. Sci. USA 96, 10 109-10 114. (doi:10.1073/pnas.96.18.10109)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96
    • Hegner, M.1    Smith, S.B.2    Bustamante, C.3
  • 106
    • 0347319178 scopus 로고    scopus 로고
    • Triple-color coincidence analysis: One step further in following higher order molecular complex formation
    • Heinze, K. G., Jahnz, M. & Schwille, P. 2004 Triple-color coincidence analysis: one step further in following higher order molecular complex formation. Biophys. J. 86, 506-516.
    • (2004) Biophys. J , vol.86 , pp. 506-516
    • Heinze, K.G.1    Jahnz, M.2    Schwille, P.3
  • 107
    • 5444270623 scopus 로고    scopus 로고
    • Concepts for nanoscale resolution in fluorescence microscopy
    • doi:10.1016/j.conb.2004. 08.015
    • Hell, S. W., Dyba, M. & Jakobs, S. 2004 Concepts for nanoscale resolution in fluorescence microscopy. Curr. Opin. Neurobiol. 14, 599-609. (doi:10.1016/j.conb.2004. 08.015)
    • (2004) Curr. Opin. Neurobiol , vol.14 , pp. 599-609
    • Hell, S.W.1    Dyba, M.2    Jakobs, S.3
  • 108
    • 33744981369 scopus 로고    scopus 로고
    • Sequence-resolved detecton of pausing by single RNA polymerase molecules
    • doi:10.1016/j.cell.2006. 04.032
    • Herbert, K. M., La Porta, A., Wong, B. J., Mooney, R. A., Neuman, K. C., Landick, R. & Block, S. M. 2006 Sequence-resolved detecton of pausing by single RNA polymerase molecules. Cell 125, 1083-1094. (doi:10.1016/j.cell.2006. 04.032)
    • (2006) Cell , vol.125 , pp. 1083-1094
    • Herbert, K.M.1    La Porta, A.2    Wong, B.J.3    Mooney, R.A.4    Neuman, K.C.5    Landick, R.6    Block, S.M.7
  • 109
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • doi:10.1038/nmeth871
    • Hinterdorfer, P. & Dufrene, Y. F. 2006 Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3, 347-355. (doi:10.1038/nmeth871)
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 110
    • 84975568363 scopus 로고
    • Optical microscopic observation of single small molecules
    • Hirschfeld, T. 1976 Optical microscopic observation of single small molecules. Appl. Opt. 15, 2965-2966.
    • (1976) Appl. Opt , vol.15 , pp. 2965-2966
    • Hirschfeld, T.1
  • 111
    • 33846099514 scopus 로고    scopus 로고
    • Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy
    • doi:10.1073/pnas.0604353104
    • Hoffmann, A. et al. 2007 Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc. Natl Acad. Sci. USA 104, 105-110. (doi:10.1073/pnas.0604353104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 105-110
    • Hoffmann, A.1
  • 112
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • doi:10.1529/biophysj. 104.043935
    • Hohng, S., Joo, C. & Ha, T. 2004 Single-molecule three-color FRET. Biophys. J. 87, 1328-1337. (doi:10.1529/biophysj. 104.043935)
    • (2004) Biophys. J , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 113
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • doi:10.1038/342154a0
    • Howard, J., Hudspeth, A. J. & Vale, R. D. 1989 Movement of microtubules by single kinesin molecules. Nature 342, 154-158. (doi:10.1038/342154a0)
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 114
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • doi:10.1038/41118
    • Hua, W., Young, E. C., Fleming, M. L. & Gelles, J. 1997 Coupling of kinesin steps to ATP hydrolysis. Nature 388, 390-393. (doi:10.1038/41118)
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Fleming, M.L.3    Gelles, J.4
  • 116
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • doi:10.1016/S0092-8674(00) 80911-3
    • Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H. & Yanagida, T. 1998 Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-171. (doi:10.1016/S0092-8674(00) 80911-3)
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 117
  • 118
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • doi:10.1038/ncb0107-7
    • Jacobson, K., Mouritsen, O. G. & Anderson, R. G. W. 2007 Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9, 7-14. (doi:10.1038/ncb0107-7)
    • (2007) Nat. Cell Biol , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 119
    • 0033462513 scopus 로고    scopus 로고
    • Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy
    • doi:10.1016/S0301-0104(99)00127-5
    • Jia, Y. W., Talaga, D. S., Lau, W. L., Lu, H. S. M., DeGrado, W. F. & Hochstrasser, R. M. 1999 Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy. Chem. Phys. 247, 69-83. (doi:10.1016/S0301-0104(99)00127-5)
    • (1999) Chem. Phys , vol.247 , pp. 69-83
    • Jia, Y.W.1    Talaga, D.S.2    Lau, W.L.3    Lu, H.S.M.4    DeGrado, W.F.5    Hochstrasser, R.M.6
  • 120
    • 33947500247 scopus 로고    scopus 로고
    • Chemical tools for biomolecular imaging
    • doi:10.1021/cb6003977
    • Johnsson, N. & Johnsson, K. 2007 Chemical tools for biomolecular imaging. ACS Chem. Biol. 2, 31-38. (doi:10.1021/cb6003977)
    • (2007) ACS Chem. Biol , vol.2 , pp. 31-38
    • Johnsson, N.1    Johnsson, K.2
  • 121
    • 33746713745 scopus 로고    scopus 로고
    • Real-time observation of RecA filament dynamics with single monomer resolution
    • doi:10.1016/j.cell.2006.06.042
    • Joo, C., McKinney, S. A., Nakamura, M., Rasnik, I., Myong, S. & Ha, T. 2006 Real-time observation of RecA filament dynamics with single monomer resolution. Cell 126, 515-527. (doi:10.1016/j.cell.2006.06.042)
    • (2006) Cell , vol.126 , pp. 515-527
    • Joo, C.1    McKinney, S.A.2    Nakamura, M.3    Rasnik, I.4    Myong, S.5    Ha, T.6
  • 122
    • 24144465824 scopus 로고    scopus 로고
    • Visualization of synaptic vesicle movement in intact synaptic boutons using fluorescence fluctuation spectroscopy
    • doi:10.1529/biophysj.105.061663
    • Jordan, R., Lemke, E. A. & Klingauf, J. 2005 Visualization of synaptic vesicle movement in intact synaptic boutons using fluorescence fluctuation spectroscopy. Biophys. J. 89, 2091-2102. (doi:10.1529/biophysj.105.061663)
    • (2005) Biophys. J , vol.89 , pp. 2091-2102
    • Jordan, R.1    Lemke, E.A.2    Klingauf, J.3
  • 123
    • 31944441873 scopus 로고    scopus 로고
    • A three-state mechanism for DNA hairpin folding characterized by multiparameter fluorescence fluctuation spectroscopy
    • doi:10.1021/ja0560736
    • Jung, J. Y. & Van Orden, A. 2006 A three-state mechanism for DNA hairpin folding characterized by multiparameter fluorescence fluctuation spectroscopy. J. Am. Chem. Soc. 128, 1240-1249. (doi:10.1021/ja0560736)
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1240-1249
    • Jung, J.Y.1    Van Orden, A.2
  • 124
    • 0037077719 scopus 로고    scopus 로고
    • Coupled rotation within single F0F1 enzyme complexes during ATP synthesis or hydrolysis
    • doi:10.1016/S0014-5793(02)03097-1
    • Kaim, G., Prummer, M., Sick, B., Zumofen, G., Renn, A., Wild, U. P. & Dimroth, P. 2002 Coupled rotation within single F0F1 enzyme complexes during ATP synthesis or hydrolysis. FEBS Lett. 525, 156-163. (doi:10.1016/S0014-5793(02)03097-1)
    • (2002) FEBS Lett , vol.525 , pp. 156-163
    • Kaim, G.1    Prummer, M.2    Sick, B.3    Zumofen, G.4    Renn, A.5    Wild, U.P.6    Dimroth, P.7
  • 125
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • doi:10.1073/pnas.0401690101
    • Kapanidis, A. N., Lee, N. K., Laurence, T. A., Doose, S., Margeat, E. & Weiss, S. 2004 Fluorescence-aided molecule sorting: analysis of structure and interactions by alternating-laser excitation of single molecules. Proc. Natl Acad. Sci. USA 101, 8936-8941. (doi:10.1073/pnas.0401690101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5    Weiss, S.6
  • 126
    • 33751212468 scopus 로고    scopus 로고
    • Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism
    • doi:10.1126/science. 1131399
    • Kapanidis, A. N., Margeat, E., Ho, S. O., Kortkhonjia, E., Weiss, S. & Ebright, R. H. 2006 Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism. Science 314, 1144-1147. (doi:10.1126/science. 1131399)
    • (2006) Science , vol.314 , pp. 1144-1147
    • Kapanidis, A.N.1    Margeat, E.2    Ho, S.O.3    Kortkhonjia, E.4    Weiss, S.5    Ebright, R.H.6
  • 127
    • 20444422552 scopus 로고    scopus 로고
    • Holliday junction dynamics and branch migration: Single-molecule analysis
    • doi:10.1073/pnas. 0407210102
    • Karymov, M., Daniel, D., Sankey, O. F. & Lyubchenko, Y. L. 2005 Holliday junction dynamics and branch migration: single-molecule analysis. Proc. Natl Acad. Sci. USA 102, 8186-8191. (doi:10.1073/pnas. 0407210102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8186-8191
    • Karymov, M.1    Daniel, D.2    Sankey, O.F.3    Lyubchenko, Y.L.4
  • 128
    • 0033598837 scopus 로고    scopus 로고
    • Fluorescence- intensity distribution analysis and its application in biomolecular detection technology
    • doi:10.1073/pnas.96.24.13756
    • Kask, P., Palo, K., Ullmann, D. & Gall, K. 1999 Fluorescence- intensity distribution analysis and its application in biomolecular detection technology. Proc. Natl Acad. Sci. USA 96, 13 756-13 761. (doi:10.1073/pnas.96.24.13756)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96
    • Kask, P.1    Palo, K.2    Ullmann, D.3    Gall, K.4
  • 129
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • doi:10.1126/science.276. 5315. 1112
    • Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L. & Bustamante, C. 1997 Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276, 1112-1116. (doi:10.1126/science.276. 5315. 1112)
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 130
    • 33750510321 scopus 로고    scopus 로고
    • Optical tweezers for force measurements on DNA in nanopores
    • 105 105-1-105 105-9, doi:10.1063/1.2358705
    • Keyser, U. F., van der Does, J., Dekker, C. & Dekker, N. H. 2006 Optical tweezers for force measurements on DNA in nanopores. Rev. Sci. Instrum. 77, 105 105-1-105 105-9. (doi:10.1063/1.2358705)
    • (2006) Rev. Sci. Instrum , vol.77
    • Keyser, U.F.1    van der Does, J.2    Dekker, C.3    Dekker, N.H.4
  • 131
    • 33344476773 scopus 로고    scopus 로고
    • Molecular recognition imaging and force spectroscopy of single biomolecules
    • doi:10.1021/ar050084m
    • Kienberger, F., Ebner, A., Gruber, H. J. & Hinterdorfer, P. 2006 Molecular recognition imaging and force spectroscopy of single biomolecules. Acc. Chem. Res. 39, 29-36. (doi:10.1021/ar050084m)
    • (2006) Acc. Chem. Res , vol.39 , pp. 29-36
    • Kienberger, F.1    Ebner, A.2    Gruber, H.J.3    Hinterdorfer, P.4
  • 132
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • doi:10.1146/annurev.bi.51. 070182.002331
    • Kim, P. S. & Baldwin, R. L. 1982 Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489. (doi:10.1146/annurev.bi.51. 070182.002331)
    • (1982) Annu. Rev. Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 133
    • 0037006790 scopus 로고    scopus 로고
    • 2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
    • doi:10.1073/ pnas.32077799
    • 2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules. Proc. Natl Acad. Sci. USA 99, 4284-4289. (doi:10.1073/ pnas.32077799)
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 4284-4289
    • Kim, H.D.1    Nienhaus, G.U.2    Ha, T.J.3    Orr, J.W.4    Williamson, J.R.5    Chu, S.6
  • 134
    • 33744502886 scopus 로고    scopus 로고
    • The initial step of DNA hairpin folding: A kinetic analysis using fluorescence correlation spectroscopy
    • doi:10.1093/nar/gkl221
    • Kim, J., Doose, S., Neuweiler, H. & Sauer, M. 2006 The initial step of DNA hairpin folding: a kinetic analysis using fluorescence correlation spectroscopy. Nucleic Acids Res. 34, 2516-2527. (doi:10.1093/nar/gkl221)
    • (2006) Nucleic Acids Res , vol.34 , pp. 2516-2527
    • Kim, J.1    Doose, S.2    Neuweiler, H.3    Sauer, M.4
  • 135
    • 0032478354 scopus 로고    scopus 로고
    • F-1-ATPase: A rotary motor made of a single molecule
    • doi:10.1016/S0092-8674(00) 81142-3
    • Kinosita, K., Yasuda, R., Noji, H., Ishiwata, S. & Yoshida, M. 1998 F-1-ATPase: a rotary motor made of a single molecule. Cell 93, 21-24. (doi:10.1016/S0092-8674(00) 81142-3)
    • (1998) Cell , vol.93 , pp. 21-24
    • Kinosita, K.1    Yasuda, R.2    Noji, H.3    Ishiwata, S.4    Yoshida, M.5
  • 136
    • 3042640723 scopus 로고    scopus 로고
    • Rotation of F-1-ATPase: How an ATP-driven molecular machine may work
    • doi:10.1146/annurev.biophys.33.110502.132716
    • Kinosita, K., Adachi, K. & Itoh, H. 2004 Rotation of F-1-ATPase: how an ATP-driven molecular machine may work. Annu. Rev. Biophys. Biomol. Struct. 33, 245-268. (doi:10.1146/annurev.biophys.33.110502.132716)
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 245-268
    • Kinosita, K.1    Adachi, K.2    Itoh, H.3
  • 137
    • 0033552942 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • doi:10.1038/16403
    • Kitamura, K., Tokunaga, M., Iwane, A. H. & Yanagida, T. 1999 A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397, 129-134. (doi:10.1038/16403)
    • (1999) Nature , vol.397 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 139
    • 0000096835 scopus 로고    scopus 로고
    • Kolb, H. C., Finn, M. G. & Sharpless, K. B. 2001 Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Edn. 40, 2004-2021. (doi:10.1002/1521-3773 (20010601)40:11〈2004: :AID-ANIE2004〉3.0.CO;2-5)
    • Kolb, H. C., Finn, M. G. & Sharpless, K. B. 2001 Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Edn. 40, 2004-2021. (doi:10.1002/1521-3773 (20010601)40:11〈2004: :AID-ANIE2004〉3.0.CO;2-5)
  • 140
    • 13844264432 scopus 로고    scopus 로고
    • Nuclear transport of single molecules: Dwell times at the nuclear pore complex
    • doi:10.1083/jcb. 200411005
    • Kubitscheck, U., Grunwald, D., Hoekstra, A., Rohleder, D., Kues, T., Siebrasse, J. P. & Peters, R. 2005 Nuclear transport of single molecules: dwell times at the nuclear pore complex. J. Cell Biol. 168, 233-243. (doi:10.1083/jcb. 200411005)
    • (2005) J. Cell Biol , vol.168 , pp. 233-243
    • Kubitscheck, U.1    Grunwald, D.2    Hoekstra, A.3    Rohleder, D.4    Kues, T.5    Siebrasse, J.P.6    Peters, R.7
  • 141
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
    • doi:10.1126/ science.1108408
    • Kural, C., Kim, H., Syed, S., Goshima, G., Gelfand, V. I. & Selvin, P. R. 2005 Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 308, 1469-1472. (doi:10.1126/ science.1108408)
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5    Selvin, P.R.6
  • 142
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • doi:10.1146/annurev.biophys. 34.040204.144637
    • Kusumi, A., Nakada, C., Ritchie, K., Murase, K., Suzuki, K., Murakoshi, H., Kasai, R. S., Kondo, J. & Fujiwara, T. 2005 Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34, 351-378. (doi:10.1146/annurev.biophys. 34.040204.144637)
    • (2005) Annu. Rev. Biophys. Biomol. Struct , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 143
    • 27344452885 scopus 로고    scopus 로고
    • Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions
    • doi:10.1073/pnas. 0507728102
    • Kuzmenkina, E. V., Heyes, C. D. & Nienhaus, G. U. 2005 Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions. Proc. Natl Acad. Sci. USA 102, 15 471-15 476. (doi:10.1073/pnas. 0507728102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 144
    • 0034687787 scopus 로고    scopus 로고
    • Fast kinetics of chromatin assembly revealed by single-molecule videomicroscopy and scanning force microscopy
    • doi:10.1073/pnas.250471597
    • Ladoux, B., Quivy, J. P., Doyle, P., du Roure, O., Almouzni, G. & Viovy, J. L. 2000 Fast kinetics of chromatin assembly revealed by single-molecule videomicroscopy and scanning force microscopy. Proc. Natl Acad. Sci. USA 97, 14 251-14 256. (doi:10.1073/pnas.250471597)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97
    • Ladoux, B.1    Quivy, J.P.2    Doyle, P.3    du Roure, O.4    Almouzni, G.5    Viovy, J.L.6
  • 145
    • 0041422345 scopus 로고    scopus 로고
    • Visualizing infection of individual influenza viruses
    • doi:10.1073/pnas.0832269100
    • Lakadamyali, M., Rust, M. J., Babcock, H. P. & Zhuang, X. W. 2003 Visualizing infection of individual influenza viruses. Proc. Natl Acad. Sci. USA 100, 9280-9285. (doi:10.1073/pnas.0832269100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9280-9285
    • Lakadamyali, M.1    Rust, M.J.2    Babcock, H.P.3    Zhuang, X.W.4
  • 147
    • 17444366080 scopus 로고    scopus 로고
    • Simultaneous, coincident optical trapping and single-molecule fluorescence
    • doi:10.1038/nmeth714
    • Lang, M. J., Fordyce, P. M., Engh, A. M., Neuman, K. C. & Block, S. M. 2004 Simultaneous, coincident optical trapping and single-molecule fluorescence. Nat. Methods 1, 133-139. (doi:10.1038/nmeth714)
    • (2004) Nat. Methods , vol.1 , pp. 133-139
    • Lang, M.J.1    Fordyce, P.M.2    Engh, A.M.3    Neuman, K.C.4    Block, S.M.5
  • 148
    • 1542306618 scopus 로고    scopus 로고
    • Photon arrival-time interval distribution (PAID): A novel tool for analyzing molecular interactions
    • doi:10.1021/ jp036499b
    • Laurence, T. A., Kapanidis, A. N., Kong, X. X., Chemla, D. S. & Weiss, S. 2004 Photon arrival-time interval distribution (PAID): a novel tool for analyzing molecular interactions. J. Phys. Chem. B 108, 3051-3067. (doi:10.1021/ jp036499b)
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3051-3067
    • Laurence, T.A.1    Kapanidis, A.N.2    Kong, X.X.3    Chemla, D.S.4    Weiss, S.5
  • 149
    • 28444431959 scopus 로고    scopus 로고
    • Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins
    • doi:10.1073/pnas.0508584102
    • Laurence, T. A., Kong, X., Jager, M. & Weiss, S. 2005 Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins. Proc. Natl Acad. Sci. USA 102, 17 348-17 353. (doi:10.1073/pnas.0508584102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102
    • Laurence, T.A.1    Kong, X.2    Jager, M.3    Weiss, S.4
  • 150
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • doi:10.1038/nature05135
    • Leake, M. C., Chandler, J. H., Wadhams, G. H., Bai, F., Berry, R. M. & Armitage, J. P. 2006 Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 443, 355-358. (doi:10.1038/nature05135)
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 151
    • 30044448463 scopus 로고    scopus 로고
    • Extreme conformational diversity in human telomeric DNA
    • doi:10.1073/ pnas.0506144102
    • Lee, J. Y., Okumus, B., Kim, D. S. & Ha, T. J. 2005a Extreme conformational diversity in human telomeric DNA. Proc. Natl Acad. Sci. USA 102, 18 938-18 943. (doi:10.1073/ pnas.0506144102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102
    • Lee, J.Y.1    Okumus, B.2    Kim, D.S.3    Ha, T.J.4
  • 152
    • 22144492905 scopus 로고    scopus 로고
    • Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation
    • doi:10.1529/biophysj.104.054114
    • Lee, N. K., Kapanidis, A. N., Wang, Y., Michalet, X., Mukhopadhyay, J., Ebright, R. H. & Weiss, S. 2005b Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation. Biophys. J. 88, 2939-2953. (doi:10.1529/biophysj.104.054114)
    • (2005) Biophys. J , vol.88 , pp. 2939-2953
    • Lee, N.K.1    Kapanidis, A.N.2    Wang, Y.3    Michalet, X.4    Mukhopadhyay, J.5    Ebright, R.H.6    Weiss, S.7
  • 153
    • 23744515834 scopus 로고    scopus 로고
    • Single-molecule optoelectronics
    • doi:10.1021/ar040146t
    • Lee, T. H., Gonzalez, J. I., Zheng, J. & Dickson, R. M. 2005c Single-molecule optoelectronics. Acc. Chem. Res. 38, 534-541. (doi:10.1021/ar040146t)
    • (2005) Acc. Chem. Res , vol.38 , pp. 534-541
    • Lee, T.H.1    Gonzalez, J.I.2    Zheng, J.3    Dickson, R.M.4
  • 154
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • doi:10.1038/nature04437
    • Lee, G., Abdi, K., Jiang, Y., Michaely, P., Bennett, V. & Marszalek, P. E. 2006a Nanospring behaviour of ankyrin repeats. Nature 440, 246-249. (doi:10.1038/nature04437)
    • (2006) Nature , vol.440 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Jiang, Y.3    Michaely, P.4    Bennett, V.5    Marszalek, P.E.6
  • 155
    • 31844453991 scopus 로고    scopus 로고
    • DNA primase acts as a molecular brake in DNA replication
    • doi:10.1038/nature04317
    • Lee, J. B., Hite, R. K., Hamdan, S. M., Xie, X. S., Richardson, C. C. & van Oijen, A. M. 2006b DNA primase acts as a molecular brake in DNA replication. Nature 439, 621-624. (doi:10.1038/nature04317)
    • (2006) Nature , vol.439 , pp. 621-624
    • Lee, J.B.1    Hite, R.K.2    Hamdan, S.M.3    Xie, X.S.4    Richardson, C.C.5    van Oijen, A.M.6
  • 156
    • 33846028172 scopus 로고    scopus 로고
    • Three-color alternating-laser excitation of single molecules: Monitoring multiple interactions and distances
    • doi:10.1529/biophysj.106. 093211
    • Lee, N. K., Kapanidis, A. N., Koh, H. R., Korlann, Y., Ho, S. O., Kim, Y., Gassman, N., Kim, S. K. & Weiss, S. 2007 Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances. Biophys. J. 92, 303-312. (doi:10.1529/biophysj.106. 093211)
    • (2007) Biophys. J , vol.92 , pp. 303-312
    • Lee, N.K.1    Kapanidis, A.N.2    Koh, H.R.3    Korlann, Y.4    Ho, S.O.5    Kim, Y.6    Gassman, N.7    Kim, S.K.8    Weiss, S.9
  • 157
    • 0032514675 scopus 로고    scopus 로고
    • RecA binding to a single double-stranded DNA molecule: A possible role of DNA conformational fluctuations
    • doi:10.1073/pnas.95.21.12295
    • Leger, J. F., Robert, J., Bourdieu, L., Chatenay, D. & Marko, J. F. 1998 RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations. Proc. Natl Acad. Sci. USA 95, 12 295-12 299. (doi:10.1073/pnas.95.21.12295)
    • (1998) Proc. Natl Acad. Sci. USA , vol.95
    • Leger, J.F.1    Robert, J.2    Bourdieu, L.3    Chatenay, D.4    Marko, J.F.5
  • 158
    • 28044454310 scopus 로고    scopus 로고
    • Single synaptic vesicle tracking in individual hippocampal boutons at rest and during synaptic activity
    • doi:10.1523/JNEUROSCI.2971-05.2005
    • Lemke, E. A. & Klingauf, J. 2005 Single synaptic vesicle tracking in individual hippocampal boutons at rest and during synaptic activity. J. Neurosci. 25, 11 034-11 044. (doi:10.1523/JNEUROSCI.2971-05.2005)
    • (2005) J. Neurosci , vol.25
    • Lemke, E.A.1    Klingauf, J.2
  • 159
    • 0003714330 scopus 로고    scopus 로고
    • Leuba, S. L. & Zlatanova, J, eds, Oxford, UK: Elsevier
    • Leuba, S. L. & Zlatanova, J. (eds) 2001 Biology at the single molecule level. Oxford, UK: Elsevier.
    • (2001) Biology at the single molecule level
  • 160
    • 0037474152 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis at high concentrations
    • doi:10.1126/science. 1079700
    • Levene, M. J., Korlach, J., Turner, S. W., Foquet, M., Craighead, H. G. & Webb, W. W. 2003 Zero-mode waveguides for single-molecule analysis at high concentrations. Science 299, 682-686. (doi:10.1126/science. 1079700)
    • (2003) Science , vol.299 , pp. 682-686
    • Levene, M.J.1    Korlach, J.2    Turner, S.W.3    Foquet, M.4    Craighead, H.G.5    Webb, W.W.6
  • 161
    • 0037399313 scopus 로고    scopus 로고
    • Ultrasensitive coincidence fluorescence detection of single DNA molecules
    • doi:10.1021/ac026367z
    • Li, H., Ying, L., Green, J. J., Balasubramanian, S. & Klenerman, D. 2003 Ultrasensitive coincidence fluorescence detection of single DNA molecules. Anal. Chem. 75, 1664-1670. (doi:10.1021/ac026367z)
    • (2003) Anal. Chem , vol.75 , pp. 1664-1670
    • Li, H.1    Ying, L.2    Green, J.J.3    Balasubramanian, S.4    Klenerman, D.5
  • 162
    • 5144220668 scopus 로고    scopus 로고
    • Measuring single-molecule nucleic acid dynamics in solution by two-color filtered ratiometric fluorescence correlation spectroscopy
    • doi:10.1073/pnas.0404 295101
    • Li, H. T., Ren, X. J., Ying, L. M., Balasubramanian, S. & Klenerman, D. 2004 Measuring single-molecule nucleic acid dynamics in solution by two-color filtered ratiometric fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 101, 14 425-14 430. (doi:10.1073/pnas.0404 295101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101
    • Li, H.T.1    Ren, X.J.2    Ying, L.M.3    Balasubramanian, S.4    Klenerman, D.5
  • 163
    • 11444262202 scopus 로고    scopus 로고
    • Rapid spontaneous accessibility of nucleosomal DNA
    • doi:10.1038/nsmb869
    • Li, G., Levitus, M., Bustamante, C. & Widom, J. 2005 Rapid spontaneous accessibility of nucleosomal DNA. Nat. Struct. Mol. Biol. 12, 46-53. (doi:10.1038/nsmb869)
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 46-53
    • Li, G.1    Levitus, M.2    Bustamante, C.3    Widom, J.4
  • 164
    • 33646131832 scopus 로고    scopus 로고
    • Probing the mechanical folding kinetics of TAR RNA by hopping, force-jump, and force-ramp methods
    • doi:10.1529/ biophysj.105.068049
    • Li, P., Collin, D., Smith, S. B., Bustamante, C. & Tinoco, I. 2006 Probing the mechanical folding kinetics of TAR RNA by hopping, force-jump, and force-ramp methods. Biophys. J. 90, 250-260. (doi:10.1529/ biophysj.105.068049)
    • (2006) Biophys. J , vol.90 , pp. 250-260
    • Li, P.1    Collin, D.2    Smith, S.B.3    Bustamante, C.4    Tinoco, I.5
  • 165
    • 84986707561 scopus 로고
    • Adsorbate deformation as a contrast mechanism in STM images of bio-polymers in an aqueous environment - images of the unstained. Hydrated DNA double helix
    • Lindsay, S. M., Thundat, T. & Nagahara, L. 1988 Adsorbate deformation as a contrast mechanism in STM images of bio-polymers in an aqueous environment - images of the unstained. Hydrated DNA double helix. J. Microsc. (Oxf) 152, 213-220.
    • (1988) J. Microsc. (Oxf) , vol.152 , pp. 213-220
    • Lindsay, S.M.1    Thundat, T.2    Nagahara, L.3
  • 166
    • 0024384378 scopus 로고
    • Images of the DNA double helix in water
    • doi:10.1126/science.2727694
    • Lindsay, S. M., Thundat, T., Nagahara, L., Knipping, U. & Rill, R. L. 1989 Images of the DNA double helix in water. Science 244, 1063-1064. (doi:10.1126/science.2727694)
    • (1989) Science , vol.244 , pp. 1063-1064
    • Lindsay, S.M.1    Thundat, T.2    Nagahara, L.3    Knipping, U.4    Rill, R.L.5
  • 169
    • 0035957720 scopus 로고    scopus 로고
    • Reversible unfolding of single RNA molecules by mechanical force
    • doi:10.1126/ science.1058498
    • Liphardt, J., Onoa, B., Smith, S. B., Tinoco, I. & Bustamante, C. 2001 Reversible unfolding of single RNA molecules by mechanical force. Science 292, 733-737. (doi:10.1126/ science.1058498)
    • (2001) Science , vol.292 , pp. 733-737
    • Liphardt, J.1    Onoa, B.2    Smith, S.B.3    Tinoco, I.4    Bustamante, C.5
  • 170
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality
    • doi:c1126/science.1071152
    • Liphardt, J., Dumont, S., Smith, S. B., Tinoco, I. & Bustamante, C. 2002 Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality. Science 296, 1832-1835. (doi:c1126/science.1071152)
    • (2002) Science , vol.296 , pp. 1832-1835
    • Liphardt, J.1    Dumont, S.2    Smith, S.B.3    Tinoco, I.4    Bustamante, C.5
  • 171
    • 0041321045 scopus 로고    scopus 로고
    • Single-molecule measurement of protein folding kinetics
    • doi:10.1126/science.1085399
    • Lipman, E. A., Schuler, B., Bakajin, O. & Eaton, W. A. 2003 Single-molecule measurement of protein folding kinetics. Science 301, 1233-1235. (doi:10.1126/science.1085399)
    • (2003) Science , vol.301 , pp. 1233-1235
    • Lipman, E.A.1    Schuler, B.2    Bakajin, O.3    Eaton, W.A.4
  • 172
    • 18744416938 scopus 로고    scopus 로고
    • Statistical evaluation of single nano-object fluorescence
    • doi:10.1002/cphc.200400560
    • Lippitz, M., Kulzer, F. & Orrit, M. 2005 Statistical evaluation of single nano-object fluorescence. Chemphyschem 6, 770-789. (doi:10.1002/cphc.200400560)
    • (2005) Chemphyschem , vol.6 , pp. 770-789
    • Lippitz, M.1    Kulzer, F.2    Orrit, M.3
  • 173
    • 34248397617 scopus 로고    scopus 로고
    • Insights on the role of nucleic acid/protein interactions in chaperoned nucleic acid rearrangements of HIV-1 reverse transcription
    • doi:10.1073/pnas.0700166104
    • Liu, H. W., Zeng, Y., Landes, C. F., Kim, Y. J., Zhu, Y., Ma, X., Vo, M. N., Musier-Forsyth, K. & Barbara, P. F. 2007 Insights on the role of nucleic acid/protein interactions in chaperoned nucleic acid rearrangements of HIV-1 reverse transcription. Proc. Natl Acad. Sci. USA 104, 5261-5267. (doi:10.1073/pnas.0700166104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5261-5267
    • Liu, H.W.1    Zeng, Y.2    Landes, C.F.3    Kim, Y.J.4    Zhu, Y.5    Ma, X.6    Vo, M.N.7    Musier-Forsyth, K.8    Barbara, P.F.9
  • 174
    • 0346057912 scopus 로고    scopus 로고
    • Single-molecule Imaging of the H-Ras membrane-anchor reveals domains in the cytoplasmic lealet of the cell membrane
    • Lommerse, P. H. M., Blab, G. A., Cognet, L., Harms, G. S., Snaar-Jagalska, B. E., Spaink, H. P. & Schmidt, T. 2004 Single-molecule Imaging of the H-Ras membrane-anchor reveals domains in the cytoplasmic lealet of the cell membrane. Biophys. J. 86, 609-616.
    • (2004) Biophys. J , vol.86 , pp. 609-616
    • Lommerse, P.H.M.1    Blab, G.A.2    Cognet, L.3    Harms, G.S.4    Snaar-Jagalska, B.E.5    Spaink, H.P.6    Schmidt, T.7
  • 175
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • doi:10.1126/science.282.5395. 1877
    • Lu, H. P., Xun, L. Y. & Xie, X. S. 1998 Single-molecule enzymatic dynamics. Science 282, 1877-1882. (doi:10.1126/science.282.5395. 1877)
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.Y.2    Xie, X.S.3
  • 176
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy
    • doi:10.1103/PhysRevLett.29.705
    • Magde, D., Elson, E. L. & Webb, W. W. 1972 Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29, 29-61. (doi:10.1103/PhysRevLett.29.705)
    • (1972) Phys. Rev. Lett , vol.29 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 177
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • doi:10.1002/bip.1974.360130103
    • Magde, D., Elson, E. L. & Webb, W. W. 1974 Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 13, 29-61. (doi:10.1002/bip.1974.360130103)
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 178
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: strategies to get along, doi:10.1016/j.cub, 10.046
    • Mallik, R. & Gross, S. P. 2004 Molecular motors: strategies to get along. Curr. Biol. 14, R971-R982. (doi:10.1016/j.cub. 2004.10.046)
    • (2004) Curr. Biol , vol.14
    • Mallik, R.1    Gross, S.P.2
  • 179
    • 15544363835 scopus 로고
    • Stretching DNA
    • doi:10.1021/ma001 30a008
    • Marko, J. F. & Siggia, E. D. 1995 Stretching DNA. Macromolecules 28, 8759-8770. (doi:10.1021/ma001 30a008)
    • (1995) Macromolecules , vol.28 , pp. 8759-8770
    • Marko, J.F.1    Siggia, E.D.2
  • 180
    • 26444552041 scopus 로고    scopus 로고
    • Length control and sharpening of atomic force microscope carbon nanotube tips assisted by an electron beam
    • doi:10.1088/0957-4484/16/11/004
    • Martinez, J., Yuzvinsky, T. D., Fennimore, A. M., Zettl, A., Garcia, R. & Bustamante, C. 2005 Length control and sharpening of atomic force microscope carbon nanotube tips assisted by an electron beam. Nanotechnology 16, 2493-2496. (doi:10.1088/0957-4484/16/11/004)
    • (2005) Nanotechnology , vol.16 , pp. 2493-2496
    • Martinez, J.1    Yuzvinsky, T.D.2    Fennimore, A.M.3    Zettl, A.4    Garcia, R.5    Bustamante, C.6
  • 181
    • 14844318136 scopus 로고    scopus 로고
    • Nanopore unzipping of individual DNA hairpin molecules
    • doi:10.1529/biophysj. 104.047274
    • Mathe, J., Visram, H., Viasnoff, V., Rabin, Y. & Meller, A. 2004 Nanopore unzipping of individual DNA hairpin molecules. Biophys. J. 87, 3205-3212. (doi:10.1529/biophysj. 104.047274)
    • (2004) Biophys. J , vol.87 , pp. 3205-3212
    • Mathe, J.1    Visram, H.2    Viasnoff, V.3    Rabin, Y.4    Meller, A.5
  • 182
    • 0037315675 scopus 로고    scopus 로고
    • Structural dynamics of individual Holliday junctions
    • doi:10.1038/nsb883
    • McKinney, S. A., Declais, A. C., Lilley, D. M. J. & Ha, T. 2003 Structural dynamics of individual Holliday junctions. Nat. Struct. Biol. 10, 93-97. (doi:10.1038/nsb883)
    • (2003) Nat. Struct. Biol , vol.10 , pp. 93-97
    • McKinney, S.A.1    Declais, A.C.2    Lilley, D.M.J.3    Ha, T.4
  • 183
    • 17644373802 scopus 로고    scopus 로고
    • Observing spontaneous branch migration of Holliday junctions one step at a time
    • doi:10.1073/pnas.0409328102
    • McKinney, S. A., Freeman, A. D. J., Lilley, D. M. J. & Ha, T. J. 2005 Observing spontaneous branch migration of Holliday junctions one step at a time. Proc. Natl Acad. Sci. USA 102, 5715-5720. (doi:10.1073/pnas.0409328102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5715-5720
    • McKinney, S.A.1    Freeman, A.D.J.2    Lilley, D.M.J.3    Ha, T.J.4
  • 184
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • doi:10.1529/biophysj.106. 082487
    • McKinney, S. A., Joo, C. & Ha, T. 2006 Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J. 91, 1941-1951. (doi:10.1529/biophysj.106. 082487)
    • (2006) Biophys. J , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 185
    • 0033548502 scopus 로고    scopus 로고
    • Single-molecule biomechanics with optical methods
    • doi:10.1126/ science.283.5408.1689
    • Mehta, A. D., Rief, M., Spudich, J. A., Smith, D. A. & Simmons, R. M. 1999 Single-molecule biomechanics with optical methods. Science 283, 1689-1695. (doi:10.1126/ science.283.5408.1689)
    • (1999) Science , vol.283 , pp. 1689-1695
    • Mehta, A.D.1    Rief, M.2    Spudich, J.A.3    Smith, D.A.4    Simmons, R.M.5
  • 186
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • doi:10.1073/pnas.0607097104
    • Merchant, K. A., Best, R. B., Louis, J. M., Gopich, I. V. & Eaton, W. A. 2007 Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc. Natl Acad. Sci. USA 104, 1528-1533. (doi:10.1073/pnas.0607097104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1528-1533
    • Merchant, K.A.1    Best, R.B.2    Louis, J.M.3    Gopich, I.V.4    Eaton, W.A.5
  • 187
    • 0028843342 scopus 로고
    • The force generated by a single kinesin molecule against an elastic load
    • doi:10.1073/pnas.92.2.574
    • Meyhofer, E. & Howard, J. 1995 The force generated by a single kinesin molecule against an elastic load. Proc. Natl Acad. Sci. USA 92, 574-578. (doi:10.1073/pnas.92.2.574)
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 574-578
    • Meyhofer, E.1    Howard, J.2
  • 188
    • 19944433260 scopus 로고    scopus 로고
    • Quantum dots for live cells, in vivo imaging, and diagnostics
    • doi:10.1126/science.1104274
    • Michalet, X. et al. 2005 Quantum dots for live cells, in vivo imaging, and diagnostics. Science 307, 538-544. (doi:10.1126/science.1104274)
    • (2005) Science , vol.307 , pp. 538-544
    • Michalet, X.1
  • 189
    • 33646937406 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of protein folding and conformational dynamics
    • doi:10.1021/ cr0404343
    • Michalet, X., Weiss, S. & Jager, M. 2006 Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem. Rev. 106, 1785-1813. (doi:10.1021/ cr0404343)
    • (2006) Chem. Rev , vol.106 , pp. 1785-1813
    • Michalet, X.1    Weiss, S.2    Jager, M.3
  • 190
    • 30944460113 scopus 로고    scopus 로고
    • Fluctuating enzymes: Lessons from single-molecule studies
    • doi:10.1021/ar040133f
    • Min, W., English, B. P., Luo, G. B., Cherayil, B. J., Kou, S. C. & Xie, X. S. 2005 Fluctuating enzymes: lessons from single-molecule studies. Acc. Chem. Res. 38, 923-931. (doi:10.1021/ar040133f)
    • (2005) Acc. Chem. Res , vol.38 , pp. 923-931
    • Min, W.1    English, B.P.2    Luo, G.B.3    Cherayil, B.J.4    Kou, S.C.5    Xie, X.S.6
  • 191
    • 0037034404 scopus 로고    scopus 로고
    • A dozen years of single-molecule spectroscopy in physics, chemistry, and biophysics
    • doi:10.1021/jp012992g
    • Moerner, W. E. 2002 A dozen years of single-molecule spectroscopy in physics, chemistry, and biophysics. J. Phys. Chem. B 106, 910-927. (doi:10.1021/jp012992g)
    • (2002) J. Phys. Chem. B , vol.106 , pp. 910-927
    • Moerner, W.E.1
  • 192
    • 0001008105 scopus 로고
    • Finding a single molecule in a haystack - optical-detection and spectroscopy of single absorbers in solids
    • Moerner, W. E. & Kador, L. 1989 Finding a single molecule in a haystack - optical-detection and spectroscopy of single absorbers in solids. Anal. Chem. 61, A1217-A1223.
    • (1989) Anal. Chem , vol.61
    • Moerner, W.E.1    Kador, L.2
  • 193
    • 0033548657 scopus 로고    scopus 로고
    • Illuminating single molecules in condensed matter
    • doi:10.1126/science. 283.5408.1670
    • Moerner, W. E. & Orrit, M. 1999 Illuminating single molecules in condensed matter. Science 283, 1670-1676. (doi:10.1126/science. 283.5408.1670)
    • (1999) Science , vol.283 , pp. 1670-1676
    • Moerner, W.E.1    Orrit, M.2
  • 194
    • 33745162550 scopus 로고    scopus 로고
    • Differential detection of dual traps improves the spatial resolution of optical tweezers
    • doi:10.1073/pnas.0603342103
    • Moffitt, J. R., Chemla, Y. R., Izhaky, D. & Bustamante, C. 2006 Differential detection of dual traps improves the spatial resolution of optical tweezers. Proc. Natl Acad. Sci. USA 103, 9006-9011. (doi:10.1073/pnas.0603342103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9006-9011
    • Moffitt, J.R.1    Chemla, Y.R.2    Izhaky, D.3    Bustamante, C.4
  • 195
    • 0030711495 scopus 로고    scopus 로고
    • Protein synthesis by chemical ligation of unprotected peptides in aqueous solution
    • Muir, T. W., Dawson, P. E. & Kent, S. B. 1997 Protein synthesis by chemical ligation of unprotected peptides in aqueous solution. Methods Enzymol. 289, 266-298.
    • (1997) Methods Enzymol , vol.289 , pp. 266-298
    • Muir, T.W.1    Dawson, P.E.2    Kent, S.B.3
  • 196
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • doi:10.1073/pnas.0611503104
    • Mukhopadhyay, S., Krishnan, R., Lemke, E. A., Lindquist, S. & Deniz, A. A. 2007 A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc. Natl Acad. Sci. USA 104, 2649-2654. (doi:10.1073/pnas.0611503104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 199
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • doi:10.1038/nature04049
    • Myong, S., Rasnik, I., Joo, C., Lohman, T. M. & Ha, T. 2005 Repetitive shuttling of a motor protein on DNA. Nature 437, 1321-1325. (doi:10.1038/nature04049)
    • (2005) Nature , vol.437 , pp. 1321-1325
    • Myong, S.1    Rasnik, I.2    Joo, C.3    Lohman, T.M.4    Ha, T.5
  • 200
    • 7544231457 scopus 로고    scopus 로고
    • Observation of internal cleavage and ligation reactions of a ribozyme
    • doi:10.1038/nsmb842
    • Nahas, M. K., Wilson, T. J., Hohng, S. C., Jarvie, K., Lilley, D. M. J. & Ha, T. 2004 Observation of internal cleavage and ligation reactions of a ribozyme. Nat. Struct. Mol. Biol. 11, 1107-1113. (doi:10.1038/nsmb842)
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1107-1113
    • Nahas, M.K.1    Wilson, T.J.2    Hohng, S.C.3    Jarvie, K.4    Lilley, D.M.J.5    Ha, T.6
  • 201
    • 30344436982 scopus 로고    scopus 로고
    • Observation of individual microtubule motor steps in living cells with endocytosed quantum dots
    • doi:10.1021/jp056360w
    • Nan, X. L., Sims, P. A., Chen, P. & Xie, X. S. 2005 Observation of individual microtubule motor steps in living cells with endocytosed quantum dots. J. Phys. Chem. B 109, 24 220-24 224. (doi:10.1021/jp056360w)
    • (2005) J. Phys. Chem. B , vol.109
    • Nan, X.L.1    Sims, P.A.2    Chen, P.3    Xie, X.S.4
  • 202
    • 0017258698 scopus 로고
    • Single-channel currents recorded from membrane of denervated frog muscle-fibers
    • doi:10.1038/260799a0
    • Neher, E. & Sakmann, B. 1976 Single-channel currents recorded from membrane of denervated frog muscle-fibers. Nature 260, 799-802. (doi:10.1038/260799a0)
    • (1976) Nature , vol.260 , pp. 799-802
    • Neher, E.1    Sakmann, B.2
  • 203
    • 33847254454 scopus 로고    scopus 로고
    • Ultrafast dynamics of protein collapse from singlemolecule photon statistics
    • doi:10.1073/pnas.0611093104
    • Nettels, D., Gopich, I. V., Hoffmann, A. & Schuler, B. 2007 Ultrafast dynamics of protein collapse from singlemolecule photon statistics. Proc. Natl Acad. Sci. USA 104, 2655-2660. (doi:10.1073/pnas.0611093104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2655-2660
    • Nettels, D.1    Gopich, I.V.2    Hoffmann, A.3    Schuler, B.4
  • 204
    • 7544235804 scopus 로고    scopus 로고
    • Optical trapping
    • doi:10.1063/1.1785844
    • Neuman, K. C. & Block, S. M. 2004 Optical trapping. Rev. Sci. Instrum. 75, 2787-2809. (doi:10.1063/1.1785844)
    • (2004) Rev. Sci. Instrum , vol.75 , pp. 2787-2809
    • Neuman, K.C.1    Block, S.M.2
  • 205
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F-1-ATPase
    • doi:10.1038/386299a0
    • Noji, H., Yasuda, R., Yoshida, M. & Kinosita, K. 1997 Direct observation of the rotation of F-1-ATPase. Nature 386, 299-302. (doi:10.1038/386299a0)
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 206
    • 1142291717 scopus 로고    scopus 로고
    • Localization accuracy in single-molecule microscopy
    • Ober, R. J., Ram, S. & Ward, E. S. 2004 Localization accuracy in single-molecule microscopy. Biophys. J. 86, 1185-1200.
    • (2004) Biophys. J , vol.86 , pp. 1185-1200
    • Ober, R.J.1    Ram, S.2    Ward, E.S.3
  • 207
    • 0034616309 scopus 로고    scopus 로고
    • Unfolding pathways of individual bacteriorhodopsins
    • doi:10.1126/science.288.5463.143
    • Oesterhelt, F., Oesterhelt, D., Pfeiffer, M., Engel, A., Gaub, H. E. & Muller, D. J. 2000 Unfolding pathways of individual bacteriorhodopsins. Science 288, 143-146. (doi:10.1126/science.288.5463.143)
    • (2000) Science , vol.288 , pp. 143-146
    • Oesterhelt, F.1    Oesterhelt, D.2    Pfeiffer, M.3    Engel, A.4    Gaub, H.E.5    Muller, D.J.6
  • 208
    • 0030809933 scopus 로고    scopus 로고
    • Mapping fluorophore distributions in three dimensions by quantitative multiple angle-total internal reflection fluorescence microscopy
    • Olveczky, B. P., Periasamy, N. & Verkman, A. S. 1997 Mapping fluorophore distributions in three dimensions by quantitative multiple angle-total internal reflection fluorescence microscopy. Biophys. J. 73, 2836-2847.
    • (1997) Biophys. J , vol.73 , pp. 2836-2847
    • Olveczky, B.P.1    Periasamy, N.2    Verkman, A.S.3
  • 209
    • 0242417558 scopus 로고    scopus 로고
    • Identifying the kinetic barriers to mechanical unfolding of the T. thermophila ribozyme
    • doi:10.1126/science.1081338
    • Onoa, B., Dumont, S., Liphardt, J., Smith, S. B., Tinoco Jr, N. & Bustamante, C. 2003 Identifying the kinetic barriers to mechanical unfolding of the T. thermophila ribozyme. Science 299, 1892-1895. (doi:10.1126/science.1081338)
    • (2003) Science , vol.299 , pp. 1892-1895
    • Onoa, B.1    Dumont, S.2    Liphardt, J.3    Smith, S.B.4    Tinoco Jr, N.5    Bustamante, C.6
  • 210
    • 0040391480 scopus 로고
    • Single pentacene molecules detected by fluorescence excitation in a para-terphenyl crystal
    • doi:10.1103/ PhysRevLett.65.2716
    • Orrit, M. & Bernard, J. 1990 Single pentacene molecules detected by fluorescence excitation in a para-terphenyl crystal. Phys Rev. Lett. 65, 2716-2719. (doi:10.1103/ PhysRevLett.65.2716)
    • (1990) Phys Rev. Lett , vol.65 , pp. 2716-2719
    • Orrit, M.1    Bernard, J.2
  • 211
    • 0033637148 scopus 로고    scopus 로고
    • Fluorescence intensity multiple distributions analysis: Concurrent determination of diffusion times and molecular brightness
    • Palo, K., Mets, U., Jager, S., Kask, P. & Gall, K. 2000 Fluorescence intensity multiple distributions analysis: concurrent determination of diffusion times and molecular brightness. Biophys. J. 79, 2858-2866.
    • (2000) Biophys. J , vol.79 , pp. 2858-2866
    • Palo, K.1    Mets, U.2    Jager, S.3    Kask, P.4    Gall, K.5
  • 212
    • 0034110795 scopus 로고    scopus 로고
    • Photobleaching in twophoton excitation microscopy
    • Patterson, G. H. & Piston, D. W. 2000 Photobleaching in twophoton excitation microscopy. Biophys. J. 78, 2159-2162.
    • (2000) Biophys. J , vol.78 , pp. 2159-2162
    • Patterson, G.H.1    Piston, D.W.2
  • 214
    • 0028766432 scopus 로고
    • Direct observation of tube-like motion of a single polymerchain
    • doi:10.1126/science. 8171335
    • Perkins, T. T., Smith, D. E. & Chu, S. 1994 Direct observation of tube-like motion of a single polymerchain. Science 264, 819-822. (doi:10.1126/science. 8171335)
    • (1994) Science , vol.264 , pp. 819-822
    • Perkins, T.T.1    Smith, D.E.2    Chu, S.3
  • 215
    • 3042733138 scopus 로고    scopus 로고
    • Freely diffusing single hairpin ribozymes provide insights into the role of secondary structure and partially folded states in RNA folding
    • doi:10.1529/biophysj.103.036087
    • Pljevaljčić, G., Millar, D. P. & Deniz, A. A. 2004 Freely diffusing single hairpin ribozymes provide insights into the role of secondary structure and partially folded states in RNA folding. Biophys. J. 87, 457-467. (doi:10.1529/biophysj.103.036087)
    • (2004) Biophys. J , vol.87 , pp. 457-467
    • Pljevaljčić, G.1    Millar, D.P.2    Deniz, A.A.3
  • 216
    • 0034709430 scopus 로고    scopus 로고
    • Single molecules of highly purified bacterial alkaline phosphatase have identical activity
    • doi:10.1021/ja994488j
    • Polakowski, R., Craig, D. B., Skelley, A. & Dovichi, N. J. 2000 Single molecules of highly purified bacterial alkaline phosphatase have identical activity. J. Am. Chem. Soc. 122, 4853-4855. (doi:10.1021/ja994488j)
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 4853-4855
    • Polakowski, R.1    Craig, D.B.2    Skelley, A.3    Dovichi, N.J.4
  • 217
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • doi:10.1083/jcb.148.5.997
    • Pralle, A., Keller, P., Florin, E. L., Simons, K. & Horber, J. K. H. 2000 Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148, 997-1007. (doi:10.1083/jcb.148.5.997)
    • (2000) J. Cell Biol , vol.148 , pp. 997-1007
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.H.5
  • 218
    • 33747133014 scopus 로고    scopus 로고
    • Developing optofluidic technology through the fusion of microfluidics and optics
    • doi:10.1038/nature05060
    • Psaltis, D., Quake, S. R. & Yang, C. H. 2006 Developing optofluidic technology through the fusion of microfluidics and optics. Nature 442, 381-386. (doi:10.1038/nature05060)
    • (2006) Nature , vol.442 , pp. 381-386
    • Psaltis, D.1    Quake, S.R.2    Yang, C.H.3
  • 219
    • 0025056742 scopus 로고
    • On the analysis of high order moments of fluorescence fluctuations
    • Qian, H. & Elson, E. L. 1990 On the analysis of high order moments of fluorescence fluctuations. Biophys. J. 57, 375-380.
    • (1990) Biophys. J , vol.57 , pp. 375-380
    • Qian, H.1    Elson, E.L.2
  • 220
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and orientations: Much to FRET about?
    • doi:10.1021/ar040138c
    • Rasnik, I., McKinney, S. A. & Ha, T. 2005 Surfaces and orientations: much to FRET about? Acc. Chem. Res. 38, 542-548. (doi:10.1021/ar040138c)
    • (2005) Acc. Chem. Res , vol.38 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 221
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long-lasting single-molecule fluorescence imaging
    • doi:10.1038/nmeth934
    • Rasnik, I., McKinney, S. A. & Ha, T. 2006 Nonblinking and long-lasting single-molecule fluorescence imaging. Nat. Methods 3, 891-893. (doi:10.1038/nmeth934)
    • (2006) Nat. Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 223
    • 33751218319 scopus 로고    scopus 로고
    • Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching
    • doi:10.1126/science.1131398
    • Revyakin, A., Liu, C. Y., Ebright, R. H. & Strick, T. R. 2006 Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching. Science 314, 1139-1143. (doi:10.1126/science.1131398)
    • (2006) Science , vol.314 , pp. 1139-1143
    • Revyakin, A.1    Liu, C.Y.2    Ebright, R.H.3    Strick, T.R.4
  • 224
    • 0037452963 scopus 로고    scopus 로고
    • Watching proteins fold one molecule at a time
    • doi:10.1073/pnas.2628068100
    • Rhoades, E., Gussakovsky, E. & Haran, G. 2003 Watching proteins fold one molecule at a time. Proc. Natl Acad. Sci. USA 100, 3197-3202. (doi:10.1073/pnas.2628068100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3197-3202
    • Rhoades, E.1    Gussakovsky, E.2    Haran, G.3
  • 225
    • 8844247109 scopus 로고    scopus 로고
    • Two-state folding observed in individual protein molecules
    • doi:10.1021/ja046209k
    • Rhoades, E., Cohen, M., Schuler, B. & Haran, G. 2004 Two-state folding observed in individual protein molecules. J. Am. Chem. Soc. 126, 14 686-14 687. (doi:10.1021/ja046209k)
    • (2004) J. Am. Chem. Soc , vol.126
    • Rhoades, E.1    Cohen, M.2    Schuler, B.3    Haran, G.4
  • 226
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • doi:10.1126/science.276.5315.1109
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M. & Gaub, H. E. 1997 Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112. (doi:10.1126/science.276.5315.1109)
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 227
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low-background-analysis of translational diffusion
    • Rigler, R., Mets, U., Widengren, J. & Kask, P. 1993 Fluorescence correlation spectroscopy with high count rate and low-background-analysis of translational diffusion. Eur. Biophys. J. Biophys. Lett. 22, 169-175.
    • (1993) Eur. Biophys. J. Biophys. Lett , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, J.3    Kask, P.4
  • 228
    • 0012331135 scopus 로고    scopus 로고
    • Rigler, R, Orrit, M. & Basche, T, eds, Berlin, Germany: Springer
    • Rigler, R., Orrit, M. & Basche, T. (eds) 2002 Single molecule spectroscopy. Berlin, Germany: Springer.
    • (2002) Single molecule spectroscopy
  • 229
    • 0037419787 scopus 로고    scopus 로고
    • Combinatorial approach to organelle-targeted fluorescent library based on the styryl scaffold
    • doi:10.1021/ja027587x
    • Rosania, G. R., Lee, J. W., Ding, L., Yoon, H. S. & Chang, Y. T. 2003 Combinatorial approach to organelle-targeted fluorescent library based on the styryl scaffold. J. Am. Chem. Soc. 125, 1130-1131. (doi:10.1021/ja027587x)
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1130-1131
    • Rosania, G.R.1    Lee, J.W.2    Ding, L.3    Yoon, H.S.4    Chang, Y.T.5
  • 230
    • 23244457898 scopus 로고    scopus 로고
    • Rotational motions of macro-molecules by single-molecule fluorescence microscopy
    • doi:10.1021/ar040137k
    • Rosenberg, S. A., Quinlan, M. E., Forkey, J. N. & Goldman, Y. E. 2005 Rotational motions of macro-molecules by single-molecule fluorescence microscopy. Acc. Chem. Res. 38, 583-593. (doi:10.1021/ar040137k)
    • (2005) Acc. Chem. Res , vol.38 , pp. 583-593
    • Rosenberg, S.A.1    Quinlan, M.E.2    Forkey, J.N.3    Goldman, Y.E.4
  • 231
    • 0037452580 scopus 로고    scopus 로고
    • Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase: Primer/template complexes
    • doi:10.1073/pnas.0434003100
    • Rothwell, P. J., Berger, S., Kensch, O., Felekyan, S., Antonik, M., Wohrl, B. M., Restle, T., Goody, R. S. & Seidel, C. A. 2003 Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase: primer/template complexes. Proc. Natl Acad. Sci. USA 100, 1655-1660. (doi:10.1073/pnas.0434003100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1655-1660
    • Rothwell, P.J.1    Berger, S.2    Kensch, O.3    Felekyan, S.4    Antonik, M.5    Wohrl, B.M.6    Restle, T.7    Goody, R.S.8    Seidel, C.A.9
  • 232
    • 3042709638 scopus 로고    scopus 로고
    • Single-molecule enzymology of RNA: Essential functional groups impact catalysis from a distance
    • doi:10.1073/pnas.0403575101
    • Rueda, D., Bokinsky, G., Rhodes, M. M., Rust, M. J., Zhuang, X. W. & Walter, N. G. 2004 Single-molecule enzymology of RNA: essential functional groups impact catalysis from a distance. Proc. Natl Acad. Sci. USA 101, 10 066-10 071. (doi:10.1073/pnas.0403575101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101
    • Rueda, D.1    Bokinsky, G.2    Rhodes, M.M.3    Rust, M.J.4    Zhuang, X.W.5    Walter, N.G.6
  • 233
    • 3142747583 scopus 로고    scopus 로고
    • Single spin detection by magnetic resonance force microscopy
    • doi:10.1038/nature02658
    • Rugar, D., Budakian, R., Mamin, H. J. & Chui, B. W. 2004 Single spin detection by magnetic resonance force microscopy. Nature 430, 329-332. (doi:10.1038/nature02658)
    • (2004) Nature , vol.430 , pp. 329-332
    • Rugar, D.1    Budakian, R.2    Mamin, H.J.3    Chui, B.W.4
  • 234
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • doi:10.1038/nsmb769
    • Rust, M. J., Lakadamyali, M., Zhang, F. & Zhuang, X. 2004 Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat. Struct. Mol. Biol. 11, 567-573. (doi:10.1038/nsmb769)
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 235
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • doi:10.1038/nmeth929
    • Rust, M. J., Bates, M. & Zhuang, X. W. 2006 Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3, 793-795. (doi:10.1038/nmeth929)
    • (2006) Nat. Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.W.3
  • 236
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • doi:10.1038/35004044
    • Sako, Y., Minoghchi, S. & Yanagida, T. 2000 Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell. Biol. 2, 168-172. (doi:10.1038/35004044)
    • (2000) Nat. Cell. Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 237
    • 13444306206 scopus 로고    scopus 로고
    • Protein unfolding and refolding under force: Methodologies for nanomechanics
    • Samori, B., Zuccheri, G. & Baschieri, P. 2005 Protein unfolding and refolding under force: methodologies for nanomechanics. Chemphyschem 6, 29-34.
    • (2005) Chemphyschem , vol.6 , pp. 29-34
    • Samori, B.1    Zuccheri, G.2    Baschieri, P.3
  • 238
    • 33645097568 scopus 로고    scopus 로고
    • Detecting molecular interactions that stabilize native bovine rhodopsin
    • doi:10.1016/j.jmb. 2006.02.008
    • Sapra, K. T., Park, P. S. H., Filipek, S., Engel, A., Muller, D. J. & Palczewski, K. 2006 Detecting molecular interactions that stabilize native bovine rhodopsin. J. Mol. Biol. 358, 255-269. (doi:10.1016/j.jmb. 2006.02.008)
    • (2006) J. Mol. Biol , vol.358 , pp. 255-269
    • Sapra, K.T.1    Park, P.S.H.2    Filipek, S.3    Engel, A.4    Muller, D.J.5    Palczewski, K.6
  • 239
    • 4444380329 scopus 로고    scopus 로고
    • Simultaneous atomic force microscope and fluorescence measurements of protein unfolding using a calibrated evanescent wave
    • doi:10.1073/pnas.0403534101
    • Sarkar, A., Robertson, R. B. & Fernandez, J. M. 2004 Simultaneous atomic force microscope and fluorescence measurements of protein unfolding using a calibrated evanescent wave. Proc. Natl Acad. Sci. USA 101, 12 882-12 886. (doi:10.1073/pnas.0403534101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101
    • Sarkar, A.1    Robertson, R.B.2    Fernandez, J.M.3
  • 240
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • doi:10.1126/science.287.5460.2007
    • Saxon, E. & Bertozzi, C. R. 2000 Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010. (doi:10.1126/science.287.5460.2007)
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 241
    • 0025867008 scopus 로고
    • Transcription by single molecules of RNA-polymerase observed by Light-Microscopy
    • doi:10.1038/352444a0
    • Schafer, D. A., Gelles, J., Sheetz, M. P. & Landick, R. 1991 Transcription by single molecules of RNA-polymerase observed by Light-Microscopy. Nature 352, 444-448. (doi:10.1038/352444a0)
    • (1991) Nature , vol.352 , pp. 444-448
    • Schafer, D.A.1    Gelles, J.2    Sheetz, M.P.3    Landick, R.4
  • 242
    • 18844471887 scopus 로고    scopus 로고
    • Identification of single molecules in aqueous solution by time-resolved fluorescence anisotropy
    • doi:10.1021/jp9833597
    • Schaffer, J., Volkmer, A., Eggeling, C., Subramaniam, V., Striker, G. & Seidel, C. A. M. 1999 Identification of single molecules in aqueous solution by time-resolved fluorescence anisotropy. J. Phys. Chem. A 103, 331-336. (doi:10.1021/jp9833597)
    • (1999) J. Phys. Chem. A , vol.103 , pp. 331-336
    • Schaffer, J.1    Volkmer, A.2    Eggeling, C.3    Subramaniam, V.4    Striker, G.5    Seidel, C.A.M.6
  • 244
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • doi:10.1038/41111
    • Schnitzer, M. J. & Block, S. M. 1997 Kinesin hydrolyses one ATP per 8-nm step. Nature 388, 386-390. (doi:10.1038/41111)
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 245
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • doi:10.1038/nature01060
    • Schuler, B., Lipman, E. A. & Eaton, W. A. 2002 Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419, 743-747. (doi:10.1038/nature01060)
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 246
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schutz, G. J., Kada, G., Pastushenko, V. P. & Schindler, H. 2000 Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J. 19, 892-901.
    • (2000) EMBO J , vol.19 , pp. 892-901
    • Schutz, G.J.1    Kada, G.2    Pastushenko, V.P.3    Schindler, H.4
  • 247
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille, P., Meyer-Almes, F. J. & Rigler, R. 1997 Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys. J. 72, 1878-1886.
    • (1997) Biophys. J , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 248
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • doi:10.1126/science. 1064103
    • Seisenberger, G., Ried, M. U., Endress, T., Buning, H., Hallek, M. & Brauchle, C. 2001 Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 294, 1929-1932. (doi:10.1126/science. 1064103)
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 249
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • doi:10.1016/S0092-8674(04)00167-9
    • Sharma, P., Varma, R., Sarasij, R. C., Ira, Gousset, K., Krishnamoorthy, G., Rao, M. & Mayor, S. 2004 Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116, 577-589. (doi:10.1016/S0092-8674(04)00167-9)
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.3    Ira, C.4    Gousset, K.5    Krishnamoorthy, G.6    Rao, M.7    Mayor, S.8
  • 250
    • 34248504534 scopus 로고    scopus 로고
    • Wide-field subdiffraction imaging by accumulated binding of diffusing probes
    • doi:10.1073/pnas.0609643104
    • Sharonov, A. & Hochstrasser, R. M. 2006 Wide-field subdiffraction imaging by accumulated binding of diffusing probes. Proc. Natl Acad. Sci. USA 103, 18 911-18 916. (doi:10.1073/pnas.0609643104)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103
    • Sharonov, A.1    Hochstrasser, R.M.2
  • 252
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: Now you see them, now you don't
    • doi:10.1038/ni1405
    • Shaw, A. S. 2006 Lipid rafts: now you see them, now you don't. Nat. Immunol. 7, 1139-1142. (doi:10.1038/ni1405)
    • (2006) Nat. Immunol , vol.7 , pp. 1139-1142
    • Shaw, A.S.1
  • 253
    • 0009982672 scopus 로고
    • Detection of single fluorescent molecules
    • doi:10.1016/0009-2614(90)85485-U
    • Shera, E. B., Seitzinger, N. K., Davis, L. M., Keller, R. A. & Soper, S. A. 1990 Detection of single fluorescent molecules. Chem. Phys. Lett. 174, 553-557. (doi:10.1016/0009-2614(90)85485-U)
    • (1990) Chem. Phys. Lett , vol.174 , pp. 553-557
    • Shera, E.B.1    Seitzinger, N.K.2    Davis, L.M.3    Keller, R.A.4    Soper, S.A.5
  • 254
    • 0033529216 scopus 로고    scopus 로고
    • RecA polymerization on double-stranded DNA by using single-molecule manipulation: The role of ATP hydrolysis
    • doi:10.1073/pnas.96.14.7916
    • Shivashankar, G. V., Feingold, M., Krichevsky, O. & Libchaber, A. 1999 RecA polymerization on double-stranded DNA by using single-molecule manipulation: the role of ATP hydrolysis. Proc. Natl Acad. Sci. USA 96, 7916-7921. (doi:10.1073/pnas.96.14.7916)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7916-7921
    • Shivashankar, G.V.1    Feingold, M.2    Krichevsky, O.3    Libchaber, A.4
  • 255
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • doi:10.1146/annurev.biophys.32.110601. 141803
    • Simons, K. & Vaz, W. L. C. 2004 Model systems, lipid rafts, and cell membranes. Annu. Rev. Biophys. Biomol. Struct. 33, 269-295. (doi:10.1146/annurev.biophys.32.110601. 141803)
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 269-295
    • Simons, K.1    Vaz, W.L.C.2
  • 256
    • 33748614065 scopus 로고    scopus 로고
    • Single molecule studies of enzyme mechanisms
    • doi:10.1021/cr0502955
    • Smiley, R. D. & Hammes, G. G. 2006 Single molecule studies of enzyme mechanisms. Chem. Rev. 106, 3080-3094. (doi:10.1021/cr0502955)
    • (2006) Chem. Rev , vol.106 , pp. 3080-3094
    • Smiley, R.D.1    Hammes, G.G.2
  • 257
    • 0026495432 scopus 로고
    • Direct mechanical measurements of the elasticity of single DNA-molecules by using magnetic beads
    • doi:10.1126/science.1439819
    • Smith, S. B., Finzi, L. & Bustamante, C. 1992 Direct mechanical measurements of the elasticity of single DNA-molecules by using magnetic beads. Science 258, 1122-1126. (doi:10.1126/science.1439819)
    • (1992) Science , vol.258 , pp. 1122-1126
    • Smith, S.B.1    Finzi, L.2    Bustamante, C.3
  • 258
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • doi:10.1126/science.271.5250. 795
    • Smith, S. B., Cui, Y. J. & Bustamante, C. 1996 Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271, 795-799. (doi:10.1126/science.271.5250. 795)
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.J.2    Bustamante, C.3
  • 259
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage phi 29 portal motor can package DNA against a large internal force
    • doi:10.1038/35099581
    • Smith, D. E., Tans, S. J., Smith, S. B., Grimes, S., Anderson, D. L. & Bustamante, C. 2001 The bacteriophage phi 29 portal motor can package DNA against a large internal force. Nature 413, 748-752. (doi:10.1038/35099581)
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 260
    • 24944503605 scopus 로고    scopus 로고
    • A molecular ruler based on plasmon coupling of single gold and silver nanoparticles
    • doi:10.1038/nbt1100
    • Sonnichsen, C., Reinhard, B. M., Liphardt, J. & Alivisatos, A. P. 2005 A molecular ruler based on plasmon coupling of single gold and silver nanoparticles. Nat. Biotechnol. 23, 741-745. (doi:10.1038/nbt1100)
    • (2005) Nat. Biotechnol , vol.23 , pp. 741-745
    • Sonnichsen, C.1    Reinhard, B.M.2    Liphardt, J.3    Alivisatos, A.P.4
  • 261
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • doi:10.1038/88611
    • Sosa, H., Peterman, E. J. G., Moerner, W. E. & Goldstein, L. S. B. 2001 ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. Nat. Struct. Biol. 8, 540-544. (doi:10.1038/88611)
    • (2001) Nat. Struct. Biol , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.G.2    Moerner, W.E.3    Goldstein, L.S.B.4
  • 262
    • 33644856865 scopus 로고    scopus 로고
    • Microsecond time scale rotation measurements of single F-1-ATPase molecules
    • doi:10.1021/bi052363n
    • Spetzler, D., York, J., Daniel, D., Fromme, R., Lowry, D. & Frasch, W. 2006 Microsecond time scale rotation measurements of single F-1-ATPase molecules. Biochemistry 45, 3117-3124. (doi:10.1021/bi052363n)
    • (2006) Biochemistry , vol.45 , pp. 3117-3124
    • Spetzler, D.1    York, J.2    Daniel, D.3    Fromme, R.4    Lowry, D.5    Frasch, W.6
  • 263
    • 24944498780 scopus 로고    scopus 로고
    • Microfluidics: Fluid physics at the nanoliter scale
    • doi:10.1103/RevModPhys.77.977
    • Squires, T. M. & Quake, S. R. 2005 Microfluidics: fluid physics at the nanoliter scale. Rev. Mod. Phys. 77, 977-1026. (doi:10.1103/RevModPhys.77.977)
    • (2005) Rev. Mod. Phys , vol.77 , pp. 977-1026
    • Squires, T.M.1    Quake, S.R.2
  • 264
    • 0032995380 scopus 로고    scopus 로고
    • Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy
    • Steyer, J. A. & Almers, W. 1999 Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy. Biophys. J. 76, 2262-2271.
    • (1999) Biophys. J , vol.76 , pp. 2262-2271
    • Steyer, J.A.1    Almers, W.2
  • 265
    • 0030855088 scopus 로고    scopus 로고
    • Transport, docking and exocytosis of single secretory granules in live chromaffin cells
    • doi:10.1038/41329
    • Steyer, J. A., Horstmann, H. & Almers, W. 1997 Transport, docking and exocytosis of single secretory granules in live chromaffin cells. Nature 388, 474-478. (doi:10.1038/41329)
    • (1997) Nature , vol.388 , pp. 474-478
    • Steyer, J.A.1    Horstmann, H.2    Almers, W.3
  • 266
    • 0029937922 scopus 로고    scopus 로고
    • The elasticity of a single supercoiled DNA molecule
    • doi:10.1126/science.271.5257.1835
    • Strick, T. R., Allemand, J. F., Bensimon, D., Bensimon, A. & Croquette, V. 1996 The elasticity of a single supercoiled DNA molecule. Science 271, 1835-1837. (doi:10.1126/science.271.5257.1835)
    • (1996) Science , vol.271 , pp. 1835-1837
    • Strick, T.R.1    Allemand, J.F.2    Bensimon, D.3    Bensimon, A.4    Croquette, V.5
  • 267
    • 0034690257 scopus 로고    scopus 로고
    • Single-molecule analysis of DNA uncoiling by a type II topoisomerase
    • doi:10.1038/35009144
    • Strick, T. R., Croquette, V. & Bensimon, D. 2000 Single-molecule analysis of DNA uncoiling by a type II topoisomerase. Nature 404, 901-904. (doi:10.1038/35009144)
    • (2000) Nature , vol.404 , pp. 901-904
    • Strick, T.R.1    Croquette, V.2    Bensimon, D.3
  • 268
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • doi:10.1016/0092- 8674(94)90060-4
    • Svoboda, K. & Block, S. M. 1994 Force and velocity measured for single kinesin molecules. Cell 77, 773-784. (doi:10.1016/0092- 8674(94)90060-4)
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 269
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • doi:10.1038/365721a0
    • Svoboda, K., Schmidt, C. F., Schnapp, B. J. & Block, S. M. 1993 Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727. (doi:10.1038/365721a0)
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 270
    • 0034876666 scopus 로고    scopus 로고
    • Single-molecule observation of protein-protein interactions in the chaperonin system
    • doi:10.1038/nbt0901-861
    • Taguchi, H., Ueno, T., Tadakuma, H., Yoshida, M. & Funatsu, T. 2001 Single-molecule observation of protein-protein interactions in the chaperonin system. Nat. Biotechnol. 19, 861-865. (doi:10.1038/nbt0901-861)
    • (2001) Nat. Biotechnol , vol.19 , pp. 861-865
    • Taguchi, H.1    Ueno, T.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 271
    • 33748267943 scopus 로고    scopus 로고
    • Information theoretical approach to single-molecule experimental design and interpretation
    • doi:10.1021/jp062192b
    • Talaga, D. S. 2006 Information theoretical approach to single-molecule experimental design and interpretation. J. Phys. Chem. A 110, 9743-9757. (doi:10.1021/jp062192b)
    • (2006) J. Phys. Chem. A , vol.110 , pp. 9743-9757
    • Talaga, D.S.1
  • 272
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • doi:10.1073/pnas.97.24.13021
    • Talaga, D. S., Lau, W. L., Roder, H., Tang, J. Y., Jia, Y. W., DeGrado, W. F. & Hochstrasser, R. M. 2000 Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl Acad. Sci. USA 97, 13 021-13 026. (doi:10.1073/pnas.97.24.13021)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97
    • Talaga, D.S.1    Lau, W.L.2    Roder, H.3    Tang, J.Y.4    Jia, Y.W.5    DeGrado, W.F.6    Hochstrasser, R.M.7
  • 273
    • 0042225050 scopus 로고    scopus 로고
    • Ten years of single-molecule spectroscopy
    • doi:10.1021/jp992505l
    • Tamarat, P., Maali, A., Lounis, B. & Orrit, M. 2000 Ten years of single-molecule spectroscopy. J. Phys. Chem. A 104, 1-16. (doi:10.1021/jp992505l)
    • (2000) J. Phys. Chem. A , vol.104 , pp. 1-16
    • Tamarat, P.1    Maali, A.2    Lounis, B.3    Orrit, M.4
  • 274
    • 0007042628 scopus 로고    scopus 로고
    • Monitoring the reactions of single enzyme molecules and single metal ions
    • doi:10.1021/ac970631k
    • Tan, W. H. & Yeung, E. S. 1997 Monitoring the reactions of single enzyme molecules and single metal ions. Anal. Chem. 69, 4242-4248. (doi:10.1021/ac970631k)
    • (1997) Anal. Chem , vol.69 , pp. 4242-4248
    • Tan, W.H.1    Yeung, E.S.2
  • 275
    • 0043009768 scopus 로고    scopus 로고
    • A four-way junction accelerates hairpin ribozyme folding via a discrete intermediate
    • doi:10.1073/pnas. 1233536100
    • Tan, E., Wilson, T. J., Nahas, M. K., Clegg, R. M., Lilley, D. M. J. & Ha, T. 2003 A four-way junction accelerates hairpin ribozyme folding via a discrete intermediate. Proc. Natl Acad. Sci. USA 100, 9308-9313. (doi:10.1073/pnas. 1233536100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9308-9313
    • Tan, E.1    Wilson, T.J.2    Nahas, M.K.3    Clegg, R.M.4    Lilley, D.M.J.5    Ha, T.6
  • 276
    • 0001579306 scopus 로고
    • Fluorescence correlation spectroscopy
    • ed. J. R. Lakowicz, New York, NY: Plenum Press
    • Thompson, N. L. 1989 Fluorescence correlation spectroscopy. In Topics in fluorescence spectroscopy, vol. 1 (ed. J. R. Lakowicz). New York, NY: Plenum Press.
    • (1989) Topics in fluorescence spectroscopy , vol.1
    • Thompson, N.L.1
  • 277
    • 0020794259 scopus 로고
    • Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy
    • Thompson, N. L. & Axelrod, D. 1983 Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 43, 103-114.
    • (1983) Biophys. J , vol.43 , pp. 103-114
    • Thompson, N.L.1    Axelrod, D.2
  • 278
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson, R. E., Larson, D. R. & Webb, W. W. 2002 Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 82, 2775-2783.
    • (2002) Biophys. J , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 279
    • 22844449759 scopus 로고    scopus 로고
    • Assembly and characterization of biomolecule-gold nanoparticle conjugates and their use in intracellular imaging
    • Tkachenko, A., Xie, H., Franzen, S. & Feldheim, D. L. 2005 Assembly and characterization of biomolecule-gold nanoparticle conjugates and their use in intracellular imaging. Methods Mol. Biol. 303, 85-99.
    • (2005) Methods Mol. Biol , vol.303 , pp. 85-99
    • Tkachenko, A.1    Xie, H.2    Franzen, S.3    Feldheim, D.L.4
  • 280
    • 14744270719 scopus 로고    scopus 로고
    • Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer
    • doi:10.1073/pnas. 0500189102
    • Tomschik, M., Zheng, H. C., van Holde, K., Zlatanova, J. & Leuba, S. H. 2005 Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA 102, 3278-3283. (doi:10.1073/pnas. 0500189102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3278-3283
    • Tomschik, M.1    Zheng, H.C.2    van Holde, K.3    Zlatanova, J.4    Leuba, S.H.5
  • 281
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • doi:10.1038/387308a0
    • Tskhovrebova, L., Trinick, J., Sleep, J. A. & Simmons, R. M. 1997 Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387, 308-312. (doi:10.1038/387308a0)
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 282
    • 2442482377 scopus 로고    scopus 로고
    • GroEL mediates protein folding with a two successive timer mechanism
    • doi:10.1016/S1097-2765(04)00261-8
    • Ueno, T., Taguchi, H., Tadakuma, H., Yoshida, M. & Funatsu, T. 2004 GroEL mediates protein folding with a two successive timer mechanism. Mol. Cell 14, 423-434. (doi:10.1016/S1097-2765(04)00261-8)
    • (2004) Mol. Cell , vol.14 , pp. 423-434
    • Ueno, T.1    Taguchi, H.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 283
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • doi:10.1038/380451a0
    • Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y. & Yanagida, T. 1996 Direct observation of single kinesin molecules moving along microtubules. Nature 380, 451-453. (doi:10.1038/380451a0)
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 284
    • 33846350208 scopus 로고    scopus 로고
    • To step or not to step? How biochemistry and mechanics influence processivity in kinesin and Eg5
    • doi:10.1016/j.ceb.2006.12.011
    • Valentine, M. T. & Gilbert, S. P. 2007 To step or not to step? How biochemistry and mechanics influence processivity in kinesin and Eg5. Curr. Opin. Cell Biol. 19, 75-81. (doi:10.1016/j.ceb.2006.12.011)
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 75-81
    • Valentine, M.T.1    Gilbert, S.P.2
  • 286
    • 0035826712 scopus 로고    scopus 로고
    • Non-Arrhenius kinetics for the loop closure of a DNA hairpin
    • doi:10.1073/pnas.101523498
    • Wallace, M. I., Ying, L. M., Balasubramanian, S. & Klenerman, D. 2001 Non-Arrhenius kinetics for the loop closure of a DNA hairpin. Proc. Natl Acad. Sci. USA 98, 5584-5589. (doi:10.1073/pnas.101523498)
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5584-5589
    • Wallace, M.I.1    Ying, L.M.2    Balasubramanian, S.3    Klenerman, D.4
  • 287
    • 33646166953 scopus 로고    scopus 로고
    • Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis
    • doi:10.1529/ biophysj.105.076224
    • Walther, K. A., Brujic, J., Li, H. B. & Fernandez, J. M. 2006 Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis. Biophys. J. 90, 3806-3812. (doi:10.1529/ biophysj.105.076224)
    • (2006) Biophys. J , vol.90 , pp. 3806-3812
    • Walther, K.A.1    Brujic, J.2    Li, H.B.3    Fernandez, J.M.4
  • 288
    • 33746607765 scopus 로고    scopus 로고
    • Single-molecule dynamics reveals cooperative binding-folding in protein recognition
    • Wang, J., Lu, Q. & Lu, H. P. 2006 Single-molecule dynamics reveals cooperative binding-folding in protein recognition. PLoS Comput. Biol. 2, 842-852.
    • (2006) PLoS Comput. Biol , vol.2 , pp. 842-852
    • Wang, J.1    Lu, Q.2    Lu, H.P.3
  • 289
    • 2942642588 scopus 로고    scopus 로고
    • Information bounds and optimal analysis of dynamic single molecule measurements
    • doi:10.1529/biophysj. 103.037739
    • Watkins, L. P. & Yang, H. 2004 Information bounds and optimal analysis of dynamic single molecule measurements. Biophys. J. 86, 4015-4029. (doi:10.1529/biophysj. 103.037739)
    • (2004) Biophys. J , vol.86 , pp. 4015-4029
    • Watkins, L.P.1    Yang, H.2
  • 290
    • 33746210086 scopus 로고    scopus 로고
    • Site-selective protein immobilization by staudinger ligation
    • doi:10.1002/anie.200502057
    • Watzke, A. et al. 2006 Site-selective protein immobilization by staudinger ligation. Angew. Chem. Int. Edn. 45, 1408-1412. (doi:10.1002/anie.200502057)
    • (2006) Angew. Chem. Int. Edn , vol.45 , pp. 1408-1412
    • Watzke, A.1
  • 291
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • doi:10.1126/science.283. 5408.1676
    • Weiss, S. 1999 Fluorescence spectroscopy of single biomolecules. Science 283, 1676-1683. (doi:10.1126/science.283. 5408.1676)
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 292
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • doi:10.1038/78941
    • Weiss, S. 2000 Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nat. Struct. Biol. 7, 724-729. (doi:10.1038/78941)
    • (2000) Nat. Struct. Biol , vol.7 , pp. 724-729
    • Weiss, S.1
  • 293
    • 0345166865 scopus 로고    scopus 로고
    • Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations
    • doi:10.1073/pnas. 2036428100
    • Weninger, K., Bowen, M. E., Chu, S. & Brunger, A. T. 2003 Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations. Proc. Natl Acad. Sci. USA 100, 14 800-14 805. (doi:10.1073/pnas. 2036428100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100
    • Weninger, K.1    Bowen, M.E.2    Chu, S.3    Brunger, A.T.4
  • 294
    • 0036106380 scopus 로고    scopus 로고
    • Salt dependence of the elasticity and overstretching transition of single DNA molecules
    • Wenner, J. R., Williams, M. C., Rouzina, I. & Bloomfield, V. A. 2002 Salt dependence of the elasticity and overstretching transition of single DNA molecules. Biophys. J. 82, 3160-3169.
    • (2002) Biophys. J , vol.82 , pp. 3160-3169
    • Wenner, J.R.1    Williams, M.C.2    Rouzina, I.3    Bloomfield, V.A.4
  • 295
    • 33645241242 scopus 로고    scopus 로고
    • Single-molecule detection and identification of multiple species by multiparameter fluorescence detection
    • doi:10.1021/ac0522759
    • Widengren, J., Kudryavtsev, V., Antonik, M., Berger, S., Gerken, M. & Seidel, C. A. 2006 Single-molecule detection and identification of multiple species by multiparameter fluorescence detection. Anal. Chem. 78, 2039-2050. (doi:10.1021/ac0522759)
    • (2006) Anal. Chem , vol.78 , pp. 2039-2050
    • Widengren, J.1    Kudryavtsev, V.2    Antonik, M.3    Berger, S.4    Gerken, M.5    Seidel, C.A.6
  • 296
    • 23744441329 scopus 로고    scopus 로고
    • Nonlinear optical chromophores as nanoscale emitters for single-molecule spectroscopy
    • doi:10.1021/ar0401294
    • Willets, K. A., Nishimura, S. Y., Schuck, P. J., Twieg, R. J. & Moerner, W. E. 2005 Nonlinear optical chromophores as nanoscale emitters for single-molecule spectroscopy. Acc. Chem. Res. 38, 549-556. (doi:10.1021/ar0401294)
    • (2005) Acc. Chem. Res , vol.38 , pp. 549-556
    • Willets, K.A.1    Nishimura, S.Y.2    Schuck, P.J.3    Twieg, R.J.4    Moerner, W.E.5
  • 297
    • 0035072057 scopus 로고    scopus 로고
    • Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching
    • Williams, M. C., Wenner, J. R., Rouzina, I. & Bloomfield, V. A. 2001a Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching. Biophys. J. 80, 1932-1939.
    • (2001) Biophys. J , vol.80 , pp. 1932-1939
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 298
    • 0035144565 scopus 로고    scopus 로고
    • Effect of pH on the overstretching transition of double-stranded DNA: Evidence of force-induced DNA melting
    • Williams, M. C., Wenner, J. R., Rouzina, L. & Bloomfield, V. A. 2001b Effect of pH on the overstretching transition of double-stranded DNA: evidence of force-induced DNA melting. Biophys. J. 80, 874-881.
    • (2001) Biophys. J , vol.80 , pp. 874-881
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, L.3    Bloomfield, V.A.4
  • 299
    • 0032573868 scopus 로고    scopus 로고
    • Carbon nanotube tips: High-resolution probes for imaging biological systems
    • doi:10.1021/ja9737735
    • Wong, S. S., Harper, J. D., Lansbury, P. T. & Lieber, C. M. 1998 Carbon nanotube tips: high-resolution probes for imaging biological systems. J. Am. Chem. Soc. 120, 603-604. (doi:10.1021/ja9737735)
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 603-604
    • Wong, S.S.1    Harper, J.D.2    Lansbury, P.T.3    Lieber, C.M.4
  • 300
    • 33750970551 scopus 로고    scopus 로고
    • Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid
    • doi:10.1126/science.1133601
    • Woodside, M. T., Anthony, P. C., Behnke-Parks, W. M., Larizadeh, K., Herschlag, D. & Block, S. M. 2006 Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid. Science 314, 1001-1004. (doi:10.1126/science.1133601)
    • (2006) Science , vol.314 , pp. 1001-1004
    • Woodside, M.T.1    Anthony, P.C.2    Behnke-Parks, W.M.3    Larizadeh, K.4    Herschlag, D.5    Block, S.M.6
  • 301
    • 0000312458 scopus 로고
    • Optical-detection of magnetic-resonance in a single molecule
    • doi:10.1038/363244a0
    • Wrachtrup, J., Vonborczyskowski, C., Bernard, J., Orrit, M. & Brown, R. 1993 Optical-detection of magnetic-resonance in a single molecule. Nature 363, 244-245. (doi:10.1038/363244a0)
    • (1993) Nature , vol.363 , pp. 244-245
    • Wrachtrup, J.1    Vonborczyskowski, C.2    Bernard, J.3    Orrit, M.4    Brown, R.5
  • 302
    • 33749019097 scopus 로고    scopus 로고
    • Innovation: A chemical toolkit for proteins - an expanded genetic code
    • doi:10.1038/nrm2005
    • Xie, J. M. & Schultz, P. G. 2006 Innovation: a chemical toolkit for proteins - an expanded genetic code. Nat. Rev. Mol. Cell Biol. 7, 775-782. (doi:10.1038/nrm2005)
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 775-782
    • Xie, J.M.1    Schultz, P.G.2
  • 303
    • 0347004715 scopus 로고    scopus 로고
    • Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme
    • doi:10.1073/pnas.2636333100
    • Xie, Z., Srividya, N., Sosnick, T. R., Pan, T. & Scherer, N. F. 2004 Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme. Proc. Natl Acad. Sci. USA 101, 534-539. (doi:10.1073/pnas.2636333100)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 534-539
    • Xie, Z.1    Srividya, N.2    Sosnick, T.R.3    Pan, T.4    Scherer, N.F.5
  • 304
    • 0028934277 scopus 로고
    • Differences in the chemical-reactivity of individual molecules of an enzyme
    • doi:10.1038/373681a0
    • Xue, Q. F. & Yeung, E. S. 1995 Differences in the chemical-reactivity of individual molecules of an enzyme. Nature 373, 681-683. (doi:10.1038/373681a0)
    • (1995) Nature , vol.373 , pp. 681-683
    • Xue, Q.F.1    Yeung, E.S.2
  • 305
    • 0037461522 scopus 로고    scopus 로고
    • Probing single-molecule dynamics photon by photon
    • doi:10.1063/1. 1521154
    • Yang, H. & Xie, X. S. 2002 Probing single-molecule dynamics photon by photon. J. Chem. Phys. 117, 10 965-10 979. (doi:10.1063/1. 1521154)
    • (2002) J. Chem. Phys , vol.117
    • Yang, H.1    Xie, X.S.2
  • 306
    • 0141993702 scopus 로고    scopus 로고
    • Protein conformational dynamics probed by single-molecule electron transfer
    • doi:10.1126/science.1086911
    • Yang, H., Luo, G., Karnchanaphanurach, P., Louie, T. M., Rech, I., Cova, S., Xun, L. & Xie, X. S. 2003 Protein conformational dynamics probed by single-molecule electron transfer. Science 302, 262-266. (doi:10.1126/science.1086911)
    • (2003) Science , vol.302 , pp. 262-266
    • Yang, H.1    Luo, G.2    Karnchanaphanurach, P.3    Louie, T.M.4    Rech, I.5    Cova, S.6    Xun, L.7    Xie, X.S.8
  • 307
    • 4444284306 scopus 로고    scopus 로고
    • Imaging of single-molecule translocation through nuclear pore complexes
    • doi:10.1073/pnas.0403675101
    • Yang, W. D., Gelles, J. & Musser, S. M. 2004 Imaging of single-molecule translocation through nuclear pore complexes. Proc. Natl Acad. Sci. USA 101, 12 887-12 892. (doi:10.1073/pnas.0403675101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101
    • Yang, W.D.1    Gelles, J.2    Musser, S.M.3
  • 308
    • 0035912221 scopus 로고    scopus 로고
    • Resolution of distinct rotational substeps by submillisecond kinetic analysis of F-1-ATPase
    • doi:10.1038/35073513
    • Yasuda, R., Noji, H., Yoshida, M., Kinosita, K. & Itoh, H. 2001 Resolution of distinct rotational substeps by submillisecond kinetic analysis of F-1-ATPase. Nature 410, 898-904. (doi:10.1038/35073513)
    • (2001) Nature , vol.410 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita, K.4    Itoh, H.5
  • 309
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • doi:10.1126/science.1084398
    • Yildiz, A., Forkey, J. N., McKinney, S. A., Ha, T., Goldman, Y. E. & Selvin, P. R. 2003 Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061-2065. (doi:10.1126/science.1084398)
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 310
    • 0942279641 scopus 로고    scopus 로고
    • Kinesin walks hand-over-hand
    • doi:10.1126/science. 1093753
    • Yildiz, A., Tomishige, M., Vale, R. D. & Selvin, P. R. 2004 Kinesin walks hand-over-hand. Science 303, 676-678. (doi:10.1126/science. 1093753)
    • (2004) Science , vol.303 , pp. 676-678
    • Yildiz, A.1    Tomishige, M.2    Vale, R.D.3    Selvin, P.R.4
  • 311
    • 0028143652 scopus 로고
    • Tethered particle motion method for studying transcript elongation by a single RNA-polymerase molecule
    • Yin, H., Landick, R. & Gelles, J. 1994 Tethered particle motion method for studying transcript elongation by a single RNA-polymerase molecule. Biophys. J. 67, 2468-2478.
    • (1994) Biophys. J , vol.67 , pp. 2468-2478
    • Yin, H.1    Landick, R.2    Gelles, J.3
  • 312
    • 0344304471 scopus 로고    scopus 로고
    • Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer
    • doi:10.1073/ pnas.2433350100
    • Ying, L. M., Green, J. J., Li, H. T., Klenerman, D. & Balasubramanian, S. 2003 Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA 100, 14 629-14 634. (doi:10.1073/ pnas.2433350100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100
    • Ying, L.M.1    Green, J.J.2    Li, H.T.3    Klenerman, D.4    Balasubramanian, S.5
  • 313
    • 33645033645 scopus 로고    scopus 로고
    • Probing gene expression in live cells, one protein molecule at a time
    • doi:10.1126/science. 1119623
    • Yu, J., Xiao, J., Ren, X. J., Lao, K. Q. & Xie, X. S. 2006 Probing gene expression in live cells, one protein molecule at a time. Science 311, 1600-1603. (doi:10.1126/science. 1119623)
    • (2006) Science , vol.311 , pp. 1600-1603
    • Yu, J.1    Xiao, J.2    Ren, X.J.3    Lao, K.Q.4    Xie, X.S.5
  • 314
    • 0034710691 scopus 로고    scopus 로고
    • Transport, capture and exocytosis of single synaptic vesicles at active zones
    • doi:10.1038/35022500
    • Zenisek, D., Steyer, J. A. & Almers, W. 2000 Transport, capture and exocytosis of single synaptic vesicles at active zones. Nature 406, 849-854. (doi:10.1038/35022500)
    • (2000) Nature , vol.406 , pp. 849-854
    • Zenisek, D.1    Steyer, J.A.2    Almers, W.3
  • 315
    • 0036902813 scopus 로고    scopus 로고
    • Creating new fluorescent probes for cell biology
    • doi:10.1038/nrm976
    • Zhang, J., Campbell, R. E., Ting, A. Y. & Tsien, R. Y. 2002 Creating new fluorescent probes for cell biology. Nat. Rev. Mol. Cell Biol. 3, 906-918. (doi:10.1038/nrm976)
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 906-918
    • Zhang, J.1    Campbell, R.E.2    Ting, A.Y.3    Tsien, R.Y.4
  • 316
    • 33947638345 scopus 로고    scopus 로고
    • DNA translocation and loop formation mechanism of chromatin remodeling by SWI/SNF and RSC
    • doi:10.1016/j.molcel.2006.10.025
    • Zhang, Y., Smith, C. L., Saha, A., Grill, S. W., Mihardja, S., Smith, S. B., Cairns, B. R., Peterson, C. L. & Bustamante, C. 2006 DNA translocation and loop formation mechanism of chromatin remodeling by SWI/SNF and RSC. Mol. Cell 24, 559-568. (doi:10.1016/j.molcel.2006.10.025)
    • (2006) Mol. Cell , vol.24 , pp. 559-568
    • Zhang, Y.1    Smith, C.L.2    Saha, A.3    Grill, S.W.4    Mihardja, S.5    Smith, S.B.6    Cairns, B.R.7    Peterson, C.L.8    Bustamante, C.9
  • 317
    • 27744505584 scopus 로고    scopus 로고
    • Fluorescence quenching by TEMPO: A sub-30 A single-molecule ruler
    • doi:10.1529/biophysj.105.071027
    • Zhu, P., Clamme, J. P. & Deniz, A. A. 2005 Fluorescence quenching by TEMPO: a sub-30 A single-molecule ruler. Biophys. J. 89, L37-L39. (doi:10.1529/biophysj.105.071027)
    • (2005) Biophys. J , vol.89
    • Zhu, P.1    Clamme, J.P.2    Deniz, A.A.3
  • 318
    • 0034674420 scopus 로고    scopus 로고
    • A single-molecule study of RNA catalysis and folding
    • doi:10.1126/science.288.5473. 2048
    • Zhuang, X. W., Bartley, L. E., Babcock, H. P., Russell, R., Ha, T. J., Herschlag, D. & Chu, S. 2000 A single-molecule study of RNA catalysis and folding. Science 288, 2048-2051. (doi:10.1126/science.288.5473. 2048)
    • (2000) Science , vol.288 , pp. 2048-2051
    • Zhuang, X.W.1    Bartley, L.E.2    Babcock, H.P.3    Russell, R.4    Ha, T.J.5    Herschlag, D.6    Chu, S.7
  • 319
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • doi:10.1126/ science.1069013
    • Zhuang, X. W., Kim, H., Pereira, M. J. B., Babcock, H. P., Walter, N. G. & Chu, S. 2002 Correlating structural dynamics and function in single ribozyme molecules. Science 296, 1473-1476. (doi:10.1126/ science.1069013)
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.W.1    Kim, H.2    Pereira, M.J.B.3    Babcock, H.P.4    Walter, N.G.5    Chu, S.6
  • 320
    • 33745606026 scopus 로고    scopus 로고
    • Subunit movements in membrane-integrated EF0F1 during ATP synthesis detected by single-molecule spectroscopy
    • doi:10.1016/j.bbabio.2006.03.020
    • Zimmermann, B., Diez, M., Borsch, M. & Graber, P. 2006 Subunit movements in membrane-integrated EF0F1 during ATP synthesis detected by single-molecule spectroscopy. Biochimica Et Biophysica Acta-Bioenergetics 1757, 311-319. (doi:10.1016/j.bbabio.2006.03.020)
    • (2006) Biochimica Et Biophysica Acta-Bioenergetics , vol.1757 , pp. 311-319
    • Zimmermann, B.1    Diez, M.2    Borsch, M.3    Graber, P.4
  • 321
    • 0037823505 scopus 로고    scopus 로고
    • Chromatin fibers, one-at-atime
    • doi:10.1016/S0022-2836 (03)00691-0
    • Zlatanova, J. & Leuba, S. H. 2003 Chromatin fibers, one-at-atime. J. Mol. Biol. 331, 1-19. (doi:10.1016/S0022-2836 (03)00691-0)
    • (2003) J. Mol. Biol , vol.331 , pp. 1-19
    • Zlatanova, J.1    Leuba, S.H.2
  • 322
    • 0034530126 scopus 로고    scopus 로고
    • Single molecule force spectroscopy in biology using the atomic force microscope
    • doi:10.1016/S0079-6107(00)00014-6
    • Zlatanova, J., Lindsay, S. M. & Leuba, S. H. 2000 Single molecule force spectroscopy in biology using the atomic force microscope. Prog. Biophys. Mol. Biol. 74, 37-61. (doi:10.1016/S0079-6107(00)00014-6)
    • (2000) Prog. Biophys. Mol. Biol , vol.74 , pp. 37-61
    • Zlatanova, J.1    Lindsay, S.M.2    Leuba, S.H.3
  • 323
    • 33744784269 scopus 로고    scopus 로고
    • Single-molecule approaches reveal the idiosyncrasies of RNA polymerases
    • doi:10.1016/j.str.2006.03.016
    • Zlatanova, J., McAllister, W. T., Borukhov, S. & Leuba, S. H. 2006 Single-molecule approaches reveal the idiosyncrasies of RNA polymerases. Structure 14, 953-966. (doi:10.1016/j.str.2006.03.016)
    • (2006) Structure , vol.14 , pp. 953-966
    • Zlatanova, J.1    McAllister, W.T.2    Borukhov, S.3    Leuba, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.