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Volumn 17, Issue 4, 2013, Pages 691-698

Making connections-strategies for single molecule fluorescence biophysics

Author keywords

[No Author keywords available]

Indexed keywords

CELL EXTRACT; FLUORESCENT DYE; RECOMBINANT PROTEIN;

EID: 84881230259     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2013.05.020     Document Type: Review
Times cited : (14)

References (50)
  • 1
    • 44449097780 scopus 로고    scopus 로고
    • Do-it-yourself guide: how to use the modern single-molecule toolkit
    • Walter N.G., Huang C.Y., Manzo A.J., Sobhy M.A. Do-it-yourself guide: how to use the modern single-molecule toolkit. Nat Methods 2008, 5:475-489.
    • (2008) Nat Methods , vol.5 , pp. 475-489
    • Walter, N.G.1    Huang, C.Y.2    Manzo, A.J.3    Sobhy, M.A.4
  • 2
    • 84859845957 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy
    • Ries J., Schwille P. Fluorescence correlation spectroscopy. BioEssays 2012, 34:361-368.
    • (2012) BioEssays , vol.34 , pp. 361-368
    • Ries, J.1    Schwille, P.2
  • 3
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman K.C., Nagy A. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat Methods 2008, 5:491-505.
    • (2008) Nat Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 4
    • 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
  • 6
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster T. Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann Phys 1948, 6:55-75.
    • (1948) Ann Phys , vol.6 , pp. 55-75
    • Förster, T.1
  • 8
    • 33645241242 scopus 로고    scopus 로고
    • Single-molecule detection and identification of multiple species by multiparameter fluorescence detection
    • Widengren J., Kudryavtsev V., Antonik M., Berger S., Gerken M., Seidel C.A. Single-molecule detection and identification of multiple species by multiparameter fluorescence detection. Anal Chem 2006, 78:2039-2050.
    • (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
  • 11
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins-an expanded genetic code
    • Xie J., Schultz P.G. A chemical toolkit for proteins-an expanded genetic code. Nat Rev Mol Cell Biol 2006, 7:775-782.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 12
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu C.C., Schultz P.G. Adding new chemistries to the genetic code. Annu Rev Biochem 2010, 79:413-444.
    • (2010) Annu Rev Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 13
    • 84863229777 scopus 로고    scopus 로고
    • Reprogramming the genetic code: from triplet to quadruplet codes
    • Wang K., Schmied W.H., Chin J.W. Reprogramming the genetic code: from triplet to quadruplet codes. Angew Chem 2012, 51:2288-2297.
    • (2012) Angew Chem , vol.51 , pp. 2288-2297
    • Wang, K.1    Schmied, W.H.2    Chin, J.W.3
  • 14
    • 70449597245 scopus 로고    scopus 로고
    • Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
    • Guo J., Melancon C.E., Lee H.S., Groff D., Schultz P.G. Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids. Angew Chem 2009, 48:9148-9151.
    • (2009) Angew Chem , vol.48 , pp. 9148-9151
    • Guo, J.1    Melancon, C.E.2    Lee, H.S.3    Groff, D.4    Schultz, P.G.5
  • 15
    • 67649656022 scopus 로고    scopus 로고
    • One plasmid selection system for the rapid evolution of aminoacyl-tRNA synthetases
    • Melancon C.E., Schultz P.G. One plasmid selection system for the rapid evolution of aminoacyl-tRNA synthetases. Bioorg Med Chem Lett 2009, 19:3845-3847.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 3845-3847
    • Melancon, C.E.1    Schultz, P.G.2
  • 16
    • 0036787635 scopus 로고    scopus 로고
    • An efficient system for the evolution of aminoacyl-tRNA synthetase specificity
    • Santoro S.W., Wang L., Herberich B., King D.S., Schultz P.G. An efficient system for the evolution of aminoacyl-tRNA synthetase specificity. Nat Biotechnol 2002, 20:1044-1048.
    • (2002) Nat Biotechnol , vol.20 , pp. 1044-1048
    • Santoro, S.W.1    Wang, L.2    Herberich, B.3    King, D.S.4    Schultz, P.G.5
  • 17
    • 34447342528 scopus 로고    scopus 로고
    • Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion
    • Wang K., Neumann H., Peak-Chew S.Y., Chin J.W. Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion. Nat Biotechnol 2007, 25:770-777.
    • (2007) Nat Biotechnol , vol.25 , pp. 770-777
    • Wang, K.1    Neumann, H.2    Peak-Chew, S.Y.3    Chin, J.W.4
  • 24
    • 77949757079 scopus 로고    scopus 로고
    • A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli
    • Huang Y., Russell W.K., Wan W., Pai P.J., Russell D.H., Liu W. A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli. Mol Biosyst 2010, 6:683-686.
    • (2010) Mol Biosyst , vol.6 , pp. 683-686
    • Huang, Y.1    Russell, W.K.2    Wan, W.3    Pai, P.J.4    Russell, D.H.5    Liu, W.6
  • 25
    • 77951568311 scopus 로고    scopus 로고
    • A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli
    • Wan W., Huang Y., Wang Z., Russell W.K., Pai P.J., Russell D.H., Liu W.R. A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli. Angew Chem 2010, 49:3211-3214.
    • (2010) Angew Chem , vol.49 , pp. 3211-3214
    • Wan, W.1    Huang, Y.2    Wang, Z.3    Russell, W.K.4    Pai, P.J.5    Russell, D.H.6    Liu, W.R.7
  • 26
    • 23044492225 scopus 로고    scopus 로고
    • Motions of the fingers subdomain of klentaq1 are fast and not rate limiting: implications for the molecular basis of fidelity in DNA polymerases
    • Rothwell P.J., Mitaksov V., Waksman G. Motions of the fingers subdomain of klentaq1 are fast and not rate limiting: implications for the molecular basis of fidelity in DNA polymerases. Mol Cell 2005, 19:345-355.
    • (2005) Mol Cell , vol.19 , pp. 345-355
    • Rothwell, P.J.1    Mitaksov, V.2    Waksman, G.3
  • 27
    • 84865729529 scopus 로고    scopus 로고
    • Intramolecular three-colour single pair FRET of intrinsically disordered proteins with increased dynamic range
    • Milles S., Koehler C., Gambin Y., Deniz A.A., Lemke E.A. Intramolecular three-colour single pair FRET of intrinsically disordered proteins with increased dynamic range. Mol Biosyst 2012, 8:2531-2534.
    • (2012) Mol Biosyst , vol.8 , pp. 2531-2534
    • Milles, S.1    Koehler, C.2    Gambin, Y.3    Deniz, A.A.4    Lemke, E.A.5
  • 30
    • 79957608770 scopus 로고    scopus 로고
    • Protein-protein interactions: pull-down for single molecules
    • Tinnefeld P. Protein-protein interactions: pull-down for single molecules. Nature 2011, 473:461-462.
    • (2011) Nature , vol.473 , pp. 461-462
    • Tinnefeld, P.1
  • 31
    • 38049077956 scopus 로고    scopus 로고
    • Visualizing the splicing of single pre-mRNA molecules in whole cell extract
    • Crawford D.J., Hoskins A.A., Friedman L.J., Gelles J., Moore M.J. Visualizing the splicing of single pre-mRNA molecules in whole cell extract. RNA 2008, 14:170-179.
    • (2008) RNA , vol.14 , pp. 170-179
    • Crawford, D.J.1    Hoskins, A.A.2    Friedman, L.J.3    Gelles, J.4    Moore, M.J.5
  • 32
    • 84864580820 scopus 로고    scopus 로고
    • Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation
    • Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., Prasanth S.G. Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation. Mol Cell Biol 2012, 32:3107-3120.
    • (2012) Mol Cell Biol , vol.32 , pp. 3107-3120
    • Shen, Z.1    Chakraborty, A.2    Jain, A.3    Giri, S.4    Ha, T.5    Prasanth, K.V.6    Prasanth, S.G.7
  • 34
    • 84871514536 scopus 로고    scopus 로고
    • Bringing single-molecule spectroscopy to macromolecular protein complexes
    • Joo C., Fareh M., Narry Kim V. Bringing single-molecule spectroscopy to macromolecular protein complexes. Trends Biochem Sci 2013, 38:30-37.
    • (2013) Trends Biochem Sci , vol.38 , pp. 30-37
    • Joo, C.1    Fareh, M.2    Narry Kim, V.3
  • 35
    • 21244458506 scopus 로고    scopus 로고
    • Lambda-Repressor oligomerization kinetics at high concentrations using fluorescence correlation spectroscopy in zero-mode waveguides
    • Samiee K.T., Foquet M., Guo L., Cox E.C., Craighead H.G. lambda-Repressor oligomerization kinetics at high concentrations using fluorescence correlation spectroscopy in zero-mode waveguides. Biophys J 2005, 88:2145-2153.
    • (2005) Biophys J , vol.88 , pp. 2145-2153
    • Samiee, K.T.1    Foquet, M.2    Guo, L.3    Cox, E.C.4    Craighead, H.G.5
  • 38
    • 39749169657 scopus 로고    scopus 로고
    • Probing transient copper Chaperone-Wilson disease protein interactions at the single-molecule level with nanovesicle trapping
    • Benítez J.J., Keller A.M., Ochieng P., Yatsunyk L.A., Huffman D.L., Rosenzweig A.C., Chen P. Probing transient copper Chaperone-Wilson disease protein interactions at the single-molecule level with nanovesicle trapping. J Am Chem Soc 2008, 130:2446-2447.
    • (2008) J Am Chem Soc , vol.130 , pp. 2446-2447
    • Benítez, J.J.1    Keller, A.M.2    Ochieng, P.3    Yatsunyk, L.A.4    Huffman, D.L.5    Rosenzweig, A.C.6    Chen, P.7
  • 39
    • 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
  • 40
    • 84867081368 scopus 로고    scopus 로고
    • A general approach to break the concentration barrier in single-molecule imaging
    • Loveland A.B., Habuchi S., Walter J.C., van Oijen A.M. A general approach to break the concentration barrier in single-molecule imaging. Nat Methods 2012, 9:987-992.
    • (2012) Nat Methods , vol.9 , pp. 987-992
    • Loveland, A.B.1    Habuchi, S.2    Walter, J.C.3    van Oijen, A.M.4
  • 45
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund P.W. Folding DNA to create nanoscale shapes and patterns. Nature 2006, 440:297-302.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.1
  • 46
  • 47
    • 83555174809 scopus 로고    scopus 로고
    • Challenges and opportunities for structural DNA nanotechnology
    • Pinheiro A.V., Han D., Shih W.M., Yan H. Challenges and opportunities for structural DNA nanotechnology. Nat Nano 2011, 6:763-772.
    • (2011) Nat Nano , vol.6 , pp. 763-772
    • Pinheiro, A.V.1    Han, D.2    Shih, W.M.3    Yan, H.4
  • 49
    • 80052929444 scopus 로고    scopus 로고
    • DNA origami: a quantum leap for self-assembly of complex structures
    • Torring T., Voigt N.V., Nangreave J., Yan H., Gothelf K.V. DNA origami: a quantum leap for self-assembly of complex structures. Chem Soc Rev 2011, 40:5636-5646.
    • (2011) Chem Soc Rev , vol.40 , pp. 5636-5646
    • Torring, T.1    Voigt, N.V.2    Nangreave, J.3    Yan, H.4    Gothelf, K.V.5
  • 50
    • 84867802881 scopus 로고    scopus 로고
    • Fluorescence enhancement at docking sites of DNA-directed self-assembled nanoantennas
    • Acuna G.P., Moller F.M., Holzmeister P., Beater S., Lalkens B., Tinnefeld P. Fluorescence enhancement at docking sites of DNA-directed self-assembled nanoantennas. Science 2012, 338:506-510.
    • (2012) Science , vol.338 , pp. 506-510
    • Acuna, G.P.1    Moller, F.M.2    Holzmeister, P.3    Beater, S.4    Lalkens, B.5    Tinnefeld, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.