메뉴 건너뛰기




Volumn 38, Issue 7, 2005, Pages 542-548

Surfaces and Orientations: Much to FRET about?

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; BOVINE SERUM ALBUMIN; SILICON DIOXIDE; STREPTAVIDIN;

EID: 23744433971     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar040138c     Document Type: Article
Times cited : (130)

References (60)
  • 1
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss, S. Fluorescence spectroscopy of single biomolecules. Science 1999, 283, 1676-1683.
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 2
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • Weiss, S. Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nat. Struct. Biol. 2000, 7, 724-729.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 724-729
    • Weiss, S.1
  • 3
    • 0041876386 scopus 로고    scopus 로고
    • Methods of single molecule fluorescence spectroscopy and microscopy
    • Moerner, W. E.; Fromm, D. P. Methods of single molecule fluorescence spectroscopy and microscopy. Rev. Sci. Instrum. 2003, 74, 3597-3619.
    • (2003) Rev. Sci. Instrum. , vol.74 , pp. 3597-3619
    • Moerner, W.E.1    Fromm, D.P.2
  • 4
    • 33645177209 scopus 로고    scopus 로고
    • Forster, T., Ed. Academic Press: New York, 1965
    • Forster, T., Ed. Academic Press: New York, 1965.
  • 6
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P. R. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 2000, 7, 730-734.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 8
    • 0034807927 scopus 로고    scopus 로고
    • Single molecule fluorescence resonance energy transfer
    • Ha, T. Single molecule fluorescence resonance energy transfer. Method 2001, 25, 78-86.
    • (2001) Method , vol.25 , pp. 78-86
    • Ha, T.1
  • 9
    • 0035366378 scopus 로고    scopus 로고
    • Single-molecule fluorescence methods for the study of nucleic acids
    • Ha, T. Single-molecule fluorescence methods for the study of nucleic acids. Curr. Opin. Struct. Biol. 2001 11, 287-292.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 287-292
    • Ha, T.1
  • 10
    • 1842583976 scopus 로고    scopus 로고
    • Structural dynamics and processing of nucleic acids revealed by single-molecule spectroscopy
    • Ha, T. Structural dynamics and processing of nucleic acids revealed by single-molecule spectroscopy. Biochemistry 2004, 43, 4055-4063.
    • (2004) Biochemistry , vol.43 , pp. 4055-4063
    • Ha, T.1
  • 11
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules - Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T.; Enderle, T.; Ogletree, D. F.; Chemla, D. S.; Selvin, P. R.; Weiss, S. Probing the interaction between two single molecules - fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 6264-6268.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 12
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signaling on the surface of living cells
    • Sako, Y.; Minoghchi, S.; Yanagida, T. Single-molecule imaging of EGFR signaling on the surface of living cells. Nat. Cell Biol. 2000, 2, 168-172.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 13
    • 0141530906 scopus 로고    scopus 로고
    • Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes
    • Nguyen, V. T.; Kamio, Y.; Higuchi, H. Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes. EMBO J. 2003, 22, 4968-4979.
    • (2003) EMBO J. , vol.22 , pp. 4968-4979
    • Nguyen, V.T.1    Kamio, Y.2    Higuchi, H.3
  • 15
    • 0033462513 scopus 로고    scopus 로고
    • Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy
    • Jia, Y. W.; Talaga, D. S.; Lau, W. L.; Lu, H. S. M.; DeGrado, W. F.; Hochstrasser, R. M. Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy. Chem. Phys. 1999, 247, 69-83.
    • (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
  • 16
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D. S.; Lau, W. L.; Roder, H.; Tang, J. Y.; Jia, Y. W.; DeGrado, W. F.; Hochstrasser, R. M. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 13021-13026.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13021-13026
    • 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
  • 17
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single- molecule fluorescence spectroscopy
    • Schuler, B.; Lipman, E. A.; Eaton, W. A. Probing the free-energy surface for protein folding with single- molecule fluorescence spectroscopy. Nature 2002, 419, 743-747.
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 19
    • 20644431583 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon
    • Brasselet, S.; Peterman, E. J. G.; Miyawaki, A.; Moerner, W. E. Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon. J. Phys. Chem. B 2000, 104, 3676-3682.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3676-3682
    • Brasselet, S.1    Peterman, E.J.G.2    Miyawaki, A.3    Moerner, W.E.4
  • 21
    • 0041923728 scopus 로고    scopus 로고
    • The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer
    • Yasuda, R.; Masaike, T.; Adachi, K.; Noji, H.; Itoh, H.; Kinosita, K., Jr. The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 9314-9318.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9314-9318
    • Yasuda, R.1    Masaike, T.2    Adachi, K.3    Noji, H.4    Itoh, H.5    Kinosita Jr., K.6
  • 22
    • 0042233472 scopus 로고    scopus 로고
    • Probing Single-Molecule T4 Lysozyme Conformational Dynamics by Intramolecular Fluorescence Energy Transfer
    • Chen, Y.; Hu, D.; Vorpagel, E. R.; Lu, H. P. Probing Single-Molecule T4 Lysozyme Conformational Dynamics by Intramolecular Fluorescence Energy Transfer. J. Phys. Chem. B 2003, 107, 7947-7956.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 7947-7956
    • Chen, Y.1    Hu, D.2    Vorpagel, E.R.3    Lu, H.P.4
  • 23
    • 0037063327 scopus 로고    scopus 로고
    • Stepwise rotation of the gamma-subunit of EF(0)F(1)-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer
    • Borsch, M.; Diez, M.; Zimmermann, B.; Reuter, R.; Graber, P. Stepwise rotation of the gamma-subunit of EF(0)F(1)-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer. FEBS Lett. 2002, 527, 147-152.
    • (2002) FEBS Lett. , vol.527 , pp. 147-152
    • Borsch, M.1    Diez, M.2    Zimmermann, B.3    Reuter, R.4    Graber, P.5
  • 29
    • 0242500997 scopus 로고    scopus 로고
    • Exploration of the transition state for tertiary structure formation between an RNA helix and a large structured RNA
    • Bartley, L. E.; Zhuang, X.; Das, R.; Chu, S.; Herschlag, D. Exploration of the transition state for tertiary structure formation between an RNA helix and a large structured RNA. J. Mol. Biol. 2003, 328, 1011-1026.
    • (2003) J. Mol. Biol. , vol.328 , pp. 1011-1026
    • Bartley, L.E.1    Zhuang, X.2    Das, R.3    Chu, S.4    Herschlag, D.5
  • 30
    • 0037006790 scopus 로고    scopus 로고
    • Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
    • Kim, H. D.; Nienhaus, G. U.; Ha, T.; Orr, J. W.; Williamson, J. R.; Chu, S. Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 4284-4289.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4284-4289
    • Kim, H.D.1    Nienhaus, G.U.2    Ha, T.3    Orr, J.W.4    Williamson, J.R.5    Chu, S.6
  • 34
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang, X. W.; Kim, H.; Pereira, M. J. B.; Babcock, H. P.; Walter, N. G.; Chu, S. Correlating structural dynamics and function in single ribozyme molecules. Science 2002, 296, 1473-1476.
    • (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
  • 35
    • 0347004715 scopus 로고    scopus 로고
    • Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme
    • Xie, Z.; Srividya, N.; Sosnick, T. R.; Pan, T.; Scherer, N. F. Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 534-539.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 534-539
    • Xie, Z.1    Srividya, N.2    Sosnick, T.R.3    Pan, T.4    Scherer, N.F.5
  • 36
  • 37
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Forster distance dependence and subpopulations
    • Deniz, A. A.; Dahan, M.; Grunwell, J. R.; Ha, T. J.; Faulhaber, A. E.; Chemla, D. S.; Weiss, S.; Schultz, P. G. Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Forster distance dependence and subpopulations. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 3670-3675.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.J.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 38
    • 0001526496 scopus 로고    scopus 로고
    • Ratiometric analysis of single-molecule fluorescence resonance energy transfer using logical combinations of threshold criteria: A study of 12-mer DNA
    • Ying, L. M.; Wallace, M. I.; Balasubramanian, S.; Klenerman, D. Ratiometric analysis of single-molecule fluorescence resonance energy transfer using logical combinations of threshold criteria: A study of 12-mer DNA. J. Phys. Chem. B 2000, 104, 5171-5178.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5171-5178
    • Ying, L.M.1    Wallace, M.I.2    Balasubramanian, S.3    Klenerman, D.4
  • 39
    • 0344304471 scopus 로고    scopus 로고
    • Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer
    • Ying, L.; Green, J. J.; Li, H.; Klenerman, D.; Balasubramanian, S. Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 14629-14634.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 14629-14634
    • Ying, L.1    Green, J.J.2    Li, H.3    Klenerman, D.4    Balasubramanian, S.5
  • 41
    • 4143055013 scopus 로고    scopus 로고
    • Exploring rare conformational species and ionic effects in DNA holliday junctions using single-molecule spectroscopy
    • Joo, C.; McKinney, S. A.; Lilley, D. M. J.; Ha, T. Exploring rare conformational species and ionic effects in DNA holliday junctions using single-molecule spectroscopy. J. Mol. Biol. 2004, 341, 739-751.
    • (2004) J. Mol. Biol. , vol.341 , pp. 739-751
    • Joo, C.1    McKinney, S.A.2    Lilley, D.M.J.3    Ha, T.4
  • 43
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and reinitiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha, T.; Rasnik, I.; Cheng, W.; Babcock, H. P.; Gauss, G.; Lohman, T. M.; Chu, S. Initiation and reinitiation of DNA unwinding by the Escherichia coli Rep helicase. Nature 2002, 479, 638-641.
    • (2002) Nature , vol.479 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Cheng, W.3    Babcock, H.P.4    Gauss, G.5    Lohman, T.M.6    Chu, S.7
  • 44
    • 0742324525 scopus 로고    scopus 로고
    • DNA-binding orientation and domain conformation of the E. coli Rep helicase monomer bound to a partial duplex junction: Single-molecule studies of fluorescently labeled enzymes
    • Rasnik, I.; Myong, S.; Cheng, W.; Lohman, T. M.; Ha, T. DNA-binding orientation and domain conformation of the E. coli Rep helicase monomer bound to a partial duplex junction: Single-molecule studies of fluorescently labeled enzymes. J. Mol. Biol. 2004, 336, 395-498.
    • (2004) J. Mol. Biol. , vol.336 , pp. 395-498
    • Rasnik, I.1    Myong, S.2    Cheng, W.3    Lohman, T.M.4    Ha, T.5
  • 46
  • 48
    • 0030832226 scopus 로고    scopus 로고
    • On/Off Blinking and Switching Behaviour of Single Molecules of Green Fluorescent Protein
    • Dickson, R. M.; Cubitt, A. B.; Tsien, R. Y.; Moerner, W. E. On/Off Blinking and Switching Behaviour of Single Molecules of Green Fluorescent Protein. Nature 1997, 388, 355-358.
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 49
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu, H. P.; Xun, L. Y.; Xie, X. S. Single-molecule enzymatic dynamics. Science 1998, 282, 1877-1882.
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.Y.2    Xie, X.S.3
  • 50
    • 0035819204 scopus 로고    scopus 로고
    • Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy
    • Boukobza, E.; Sonnenfeld, A.; Haran, G. Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy. J. Phys. Chem. B 2001, 105, 12165-12170.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12165-12170
    • Boukobza, E.1    Sonnenfeld, A.2    Haran, G.3
  • 51
    • 7544225920 scopus 로고    scopus 로고
    • Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic
    • Okumus, B.; Wilson, T. J.; Lilley, D. M. J.; Ha, T. Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic. Biophys. J. 2004, 87, 2798-2806.
    • (2004) Biophys. J. , vol.87 , pp. 2798-2806
    • Okumus, B.1    Wilson, T.J.2    Lilley, D.M.J.3    Ha, T.4
  • 52
    • 0032115878 scopus 로고    scopus 로고
    • Poly(ethylen oxide) grafted to silicon surfaces: Grafting density and protein adsorption
    • Sofia, S. J., Premnath, V.; Merrill, E. W. Poly(ethylen oxide) grafted to silicon surfaces: grafting density and protein adsorption. Macromolecules 1998, 31, 5059.
    • (1998) Macromolecules , vol.31 , pp. 5059
    • Sofia, S.J.1    Premnath, V.2    Merrill, E.W.3
  • 53
    • 0026351910 scopus 로고
    • Self-Assembled Organic Monolayers: Model Systems for Studying Adsorption of Proteins at Surfaces
    • Prime, K. L.; Whitesides, G. M. Self-Assembled Organic Monolayers: Model Systems for Studying Adsorption of Proteins at Surfaces. Science 1991, 252, 1164.
    • (1991) Science , vol.252 , pp. 1164
    • Prime, K.L.1    Whitesides, G.M.2
  • 54
    • 1842607369 scopus 로고    scopus 로고
    • Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins
    • Groll, J.; Amirgoulova, E. V.; Ameringer, T.; Heyes, C. D.; Rocker, C.; Nienhaus, G. U.; Moller, M. Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins. J. Am. Chem. Soc. 2004, 126, 4234-4239.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4234-4239
    • Groll, J.1    Amirgoulova, E.V.2    Ameringer, T.3    Heyes, C.D.4    Rocker, C.5    Nienhaus, G.U.6    Moller, M.7
  • 55
    • 3042709638 scopus 로고    scopus 로고
    • Single-molecule enzymology of RNA: Essential functional groups impact catalysis from a distance
    • Rueda, D.; Bokinsky, G.; Rhodes, M. M.; Rust, M. J.; Zhuang, X.; Walter, N. G. Single-molecule enzymology of RNA: essential functional groups impact catalysis from a distance. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 10066-10071.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10066-10071
    • Rueda, D.1    Bokinsky, G.2    Rhodes, M.M.3    Rust, M.J.4    Zhuang, X.5    Walter, N.G.6
  • 56
    • 0001759698 scopus 로고    scopus 로고
    • Simultaneous dual-color and dual-polarization imaging of single molecules
    • Cognet, L.; Harms, G. S.; Blab, G. A.; Lommerse, P. H. M.; Schmidt, T. Simultaneous dual-color and dual-polarization imaging of single molecules. Appl. Phys. Lett. 2000, 77, 4052-4054.
    • (2000) Appl. Phys. Lett. , vol.77 , pp. 4052-4054
    • Cognet, L.1    Harms, G.S.2    Blab, G.A.3    Lommerse, P.H.M.4    Schmidt, T.5
  • 57
    • 0030740262 scopus 로고    scopus 로고
    • Major Domain Swiveling Revealed by the Crystal Structures of Complexes of E-Coli Rep Helicase Bound to Single-Stranded DNA and ATP
    • Korolev, S.; Hsieh, J.; Gauss, G. H.; Lohman, T. M.; Waksman, G. Major Domain Swiveling Revealed By the Crystal Structures of Complexes of E-Coli Rep Helicase Bound to Single-Stranded DNA and ATP. Cell 1997, 90, 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 58
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S.; Soultanas, P.; Dillingham, M. S.; Subramanya, H. S.; Wigley, D. B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 1999, 97, 75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 59
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule Three-color FRET
    • Hohng, S.; Joo, C.; Ha, T. Single-molecule Three-color FRET. Biophys. J. 2004, 87, 1328-1337.
    • (2004) Biophys. J. , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 60
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • Kapanidis, A. N.; Lee, N. K.; Laurence, T. A.; Doose, S.; Margeat, E.; Weiss, S. Fluorescence-aided molecule sorting: analysis of structure and interactions by alternating-laser excitation of single molecules. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 8936-8941.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.