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Volumn 18, Issue 1, 2008, Pages 16-26

Protein folding studied by single-molecule FRET

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; REVIEW; THEORETICAL MODEL; THERMODYNAMICS;

EID: 39149087014     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.12.003     Document Type: Review
Times cited : (570)

References (84)
  • 4
    • 33846940059 scopus 로고    scopus 로고
    • Mechanical unfolding of proteins: insights into biology, structure and folding
    • Forman J.R., and Clarke J. Mechanical unfolding of proteins: insights into biology, structure and folding. Curr Opin Struct Biol 17 (2007) 58-66
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 58-66
    • Forman, J.R.1    Clarke, J.2
  • 5
    • 23744478437 scopus 로고    scopus 로고
    • Free energy surfaces from single-molecule force spectroscopy
    • Hummer G., and Szabo A. Free energy surfaces from single-molecule force spectroscopy. Accounts Chem Res 38 (2005) 504-513
    • (2005) Accounts Chem Res , vol.38 , pp. 504-513
    • Hummer, G.1    Szabo, A.2
  • 6
    • 0042287973 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of biomolecular folding
    • Haran G. Single-molecule fluorescence spectroscopy of biomolecular folding. J Phys Condens Matter 15 (2003) R1291-R1317
    • (2003) J Phys Condens Matter , vol.15
    • Haran, G.1
  • 7
    • 22444436718 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of protein folding
    • Schuler B. Single-molecule fluorescence spectroscopy of protein folding. Chemphyschem 6 (2005) 1206-1220
    • (2005) Chemphyschem , vol.6 , pp. 1206-1220
    • Schuler, B.1
  • 8
    • 33646937406 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of protein folding and conformational dynamics
    • Michalet X., Weiss S., and Jäger M. Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem Rev 106 (2006) 1785-1813
    • (2006) Chem Rev , vol.106 , pp. 1785-1813
    • Michalet, X.1    Weiss, S.2    Jäger, M.3
  • 9
    • 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., and 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 93 (1996) 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
  • 10
    • 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., and Hochstrasser R.M. Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy. Chem Phys 247 (1999) 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
  • 11
    • 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., Jia Y., DeGrado W.F., and 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 97 (2000) 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.4    Jia, Y.5    DeGrado, W.F.6    Hochstrasser, R.M.7
  • 13
    • 3042538758 scopus 로고    scopus 로고
    • Using photoinduced charge transfer reactions to study conformational dynamics of biopolymers at the single-molecule level
    • Neuweiler H., and Sauer M. Using photoinduced charge transfer reactions to study conformational dynamics of biopolymers at the single-molecule level. Curr Pharm Biotechnol 5 (2004) 285-298
    • (2004) Curr Pharm Biotechnol , vol.5 , pp. 285-298
    • Neuweiler, H.1    Sauer, M.2
  • 14
    • 0036400525 scopus 로고    scopus 로고
    • What fluorescence correlation spectroscopy can tell us about unfolded proteins
    • Frieden C., Chattopadhyay K., and Elson E.L. What fluorescence correlation spectroscopy can tell us about unfolded proteins. Adv Protein Chem 62 (2002) 91-109
    • (2002) Adv Protein Chem , vol.62 , pp. 91-109
    • Frieden, C.1    Chattopadhyay, K.2    Elson, E.L.3
  • 15
    • 20544464457 scopus 로고    scopus 로고
    • How well can simulation predict protein folding kinetics and thermodynamics?
    • Snow C.D., Sorin E.J., Rhee Y.M., and Pande V.S. How well can simulation predict protein folding kinetics and thermodynamics?. Annu Rev Biophys Biomol Struct 34 (2005) 43-69
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 43-69
    • Snow, C.D.1    Sorin, E.J.2    Rhee, Y.M.3    Pande, V.S.4
  • 16
    • 33644986099 scopus 로고    scopus 로고
    • Mechanisms of protein assembly: lessons from minimalist models
    • Levy Y., and Onuchic J.N. Mechanisms of protein assembly: lessons from minimalist models. Acc Chem Res 39 (2006) 135-142
    • (2006) Acc Chem Res , vol.39 , pp. 135-142
    • Levy, Y.1    Onuchic, J.N.2
  • 18
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • Oliveberg M., and Wolynes P.G. The experimental survey of protein-folding energy landscapes. Q Rev Biophys 38 (2005) 245-288
    • (2005) Q Rev Biophys , vol.38 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 19
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht A.R., and Daggett V. Protein folding and unfolding at atomic resolution. Cell 108 (2002) 573-582
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 20
    • 8644232696 scopus 로고    scopus 로고
    • Combinatorial modeling of protein folding kinetics: free energy profiles and rates
    • Henry E.R., and Eaton W.A. Combinatorial modeling of protein folding kinetics: free energy profiles and rates. Chem Phys 307 (2004) 163-185
    • (2004) Chem Phys , vol.307 , pp. 163-185
    • Henry, E.R.1    Eaton, W.A.2
  • 21
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster T. Zwischenmolekulare Energiewanderung und Fluoreszenz. Annalen der Physik 6 (1948) 55-75
    • (1948) Annalen der Physik , vol.6 , pp. 55-75
    • Förster, T.1
  • 22
    • 14544283620 scopus 로고    scopus 로고
    • Polyproline and the "spectroscopic ruler" revisited with single molecule fluorescence
    • Schuler B., Lipman E.A., Steinbach P.J., Kumke M., and Eaton W.A. Polyproline and the "spectroscopic ruler" revisited with single molecule fluorescence. Proc Natl Acad Sci U S A 102 (2005) 2754-2759
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2754-2759
    • Schuler, B.1    Lipman, E.A.2    Steinbach, P.J.3    Kumke, M.4    Eaton, W.A.5
  • 24
    • 33646416480 scopus 로고    scopus 로고
    • Quantitative single-molecule conformational distributions: a case study with poly-(l-proline)
    • Watkins L.P., Chang H.Y., and Yang H. Quantitative single-molecule conformational distributions: a case study with poly-(l-proline). J Phys Chem A 110 (2006) 5191-5203
    • (2006) J Phys Chem A , vol.110 , pp. 5191-5203
    • Watkins, L.P.1    Chang, H.Y.2    Yang, H.3
  • 25
    • 36849083388 scopus 로고    scopus 로고
    • Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix
    • Doose S., Neuweiler H., Barsch H., and Sauer M. Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix. Proc Natl Acad Sci U S A 104 (2007) 17400-17405
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17400-17405
    • Doose, S.1    Neuweiler, H.2    Barsch, H.3    Sauer, M.4
  • 26
    • 37649015345 scopus 로고    scopus 로고
    • Best R, Merchant K, Gopich IV, Schuler B, Bax A, Eaton WA: Effect of flexibility and cis residues in single molecule FRET studies of polyproline. Proc Natl Acad Sci U S A 2007, 104:18964-18969.
    • Best R, Merchant K, Gopich IV, Schuler B, Bax A, Eaton WA: Effect of flexibility and cis residues in single molecule FRET studies of polyproline. Proc Natl Acad Sci U S A 2007, 104:18964-18969. A combination of single-molecule intensity and subpopulation lifetime measurements, NMR, and molecular dynamics simulations of polyproline, including the dyes and their linkers to the polypeptide, shows that that the kinks arising from internal cis-prolines are primarily responsible for a mean FRET efficiency higher than predicted for a rigid-rod all-trans polyproline. Theoretical analysis also shows that the width in excess of shot noise in the observed efficiency histograms and distributions of donor fluorescence lifetimes are explained by the presence of multiple species with efficiencies consistent with the simulations and the populations from NMR.
  • 28
    • 33646377416 scopus 로고    scopus 로고
    • Separating structural heterogeneities from stochastic variations in fluorescence resonance energy transfer distributions via photon distribution analysis
    • Antonik M., Felekyan S., Gaiduk A., and Seidel C.A.M. Separating structural heterogeneities from stochastic variations in fluorescence resonance energy transfer distributions via photon distribution analysis. J Phys Chem B 110 (2006) 6970-6978
    • (2006) J Phys Chem B , vol.110 , pp. 6970-6978
    • Antonik, M.1    Felekyan, S.2    Gaiduk, A.3    Seidel, C.A.M.4
  • 29
    • 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., and 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 101 (2004) 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
  • 30
    • 22144492905 scopus 로고    scopus 로고
    • Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation
    • Lee N.K., Kapanidis A.N., Wang Y., Michalet X., Mukhopadhyay J., Ebright R.H., and Weiss S. Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation. Biophys J 88 (2005) 2939-2953
    • (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
  • 31
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • The unfolded subpopulations of protein L and CspTm are compared over a range of denaturant concentrations from FRET efficiencies determined from both intensity and lifetime measurements. The interpretation is guided by Langevin simulations of a simplified representation of the polypeptide, which also suggest that collapse can result either from increased inter-residue attraction or from decreased excluded volume.
    • Merchant K.A., Best R.B., Louis J.M., Gopich I.V., and Eaton W.A. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc Natl Acad Sci U S A 104 (2007) 1528-1533. The unfolded subpopulations of protein L and CspTm are compared over a range of denaturant concentrations from FRET efficiencies determined from both intensity and lifetime measurements. The interpretation is guided by Langevin simulations of a simplified representation of the polypeptide, which also suggest that collapse can result either from increased inter-residue attraction or from decreased excluded volume.
    • (2007) Proc Natl Acad Sci U S A , 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
  • 32
    • 33644767158 scopus 로고    scopus 로고
    • Single-molecule FRET study of denaturant induced unfolding of RNase H
    • Kuzmenkina E.V., Heyes C.D., and Nienhaus G.U. Single-molecule FRET study of denaturant induced unfolding of RNase H. J Mol Biol 357 (2006) 313-324
    • (2006) J Mol Biol , vol.357 , pp. 313-324
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 33
    • 0037566231 scopus 로고    scopus 로고
    • Single-macromolecule fluorescence resonance energy transfer and free-energy profiles
    • Gopich I.V., and Szabo A. Single-macromolecule fluorescence resonance energy transfer and free-energy profiles. J Phys Chem B 107 (2003) 5058-5063
    • (2003) J Phys Chem B , vol.107 , pp. 5058-5063
    • Gopich, I.V.1    Szabo, A.2
  • 34
    • 34548096938 scopus 로고    scopus 로고
    • Theory of photon statistics in single-molecule Förster resonance energy transfer
    • Gopich I.V., and Szabo A. Theory of photon statistics in single-molecule Förster resonance energy transfer. J Chem Phys 122 (2005) 1-18
    • (2005) J Chem Phys , vol.122 , pp. 1-18
    • Gopich, I.V.1    Szabo, A.2
  • 35
    • 36249028655 scopus 로고    scopus 로고
    • Single-molecule FRET with diffusion and conformational dynamics
    • A comprehensive theory is presented for the analysis of single-molecule FRET measurements on freely diffusing and immobilized molecules, including the contribution of various processes to the distribution and variance in FRET efficiency.
    • Gopich I.V., and Szabo A. Single-molecule FRET with diffusion and conformational dynamics. J Phys Chem B 111 (2007) 12925-12932. A comprehensive theory is presented for the analysis of single-molecule FRET measurements on freely diffusing and immobilized molecules, including the contribution of various processes to the distribution and variance in FRET efficiency.
    • (2007) J Phys Chem B , vol.111 , pp. 12925-12932
    • Gopich, I.V.1    Szabo, A.2
  • 36
    • 28444431959 scopus 로고    scopus 로고
    • Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins
    • This work contains the first use of subpopulation-specific fluorescence lifetime analysis for the investigation of distance distributions in unfolded proteins and infers the presence of transient unfolded state structure in CI2 and ACBP.
    • Laurence T.A., Kong X.X., Jäger M., and Weiss S. Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins. Proc Natl Acad Sci U S A 102 (2005) 17348-17353. This work contains the first use of subpopulation-specific fluorescence lifetime analysis for the investigation of distance distributions in unfolded proteins and infers the presence of transient unfolded state structure in CI2 and ACBP.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17348-17353
    • Laurence, T.A.1    Kong, X.X.2    Jäger, M.3    Weiss, S.4
  • 37
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler B., Lipman E.A., and Eaton W.A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419 (2002) 743-747
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 38
    • 33846099514 scopus 로고    scopus 로고
    • Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy
    • By varying the position of donor and acceptor in the chain, different segments of unfolded CspTm are probed, indicating isotropic collapse and good agreement with Gaussian-chain behavior even in the collapsed unfolded state. Synchrotron circular dichroism spectroscopy reveals the formation of some β-structure concomitant with collapse.
    • Hoffmann A., Kane A., Nettels D., Hertzog D.E., Baumgärtel P., Lengefeld J., Reichardt G., Horsley D.A., Seckler R., Bakajin O., and Schuler B. Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc Natl Acad Sci U S A 104 (2007) 105-110. By varying the position of donor and acceptor in the chain, different segments of unfolded CspTm are probed, indicating isotropic collapse and good agreement with Gaussian-chain behavior even in the collapsed unfolded state. Synchrotron circular dichroism spectroscopy reveals the formation of some β-structure concomitant with collapse.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 105-110
    • Hoffmann, A.1    Kane, A.2    Nettels, D.3    Hertzog, D.E.4    Baumgärtel, P.5    Lengefeld, J.6    Reichardt, G.7    Horsley, D.A.8    Seckler, R.9    Bakajin, O.10    Schuler, B.11
  • 39
    • 27344452885 scopus 로고    scopus 로고
    • Single-molecule Förster resonance energy transfer study of protein dynamics under denaturing conditions
    • Folding/unfolding trajectories are obtained from FRET efficiency measurements on surface-immobilized RNase H, and suggest unfolded state dynamics on time scales from microseconds to seconds.
    • Kuzmenkina E.V., Heyes C.D., and Nienhaus G.U. Single-molecule Förster resonance energy transfer study of protein dynamics under denaturing conditions. Proc Natl Acad Sci U S A 102 (2005) 15471-15476. Folding/unfolding trajectories are obtained from FRET efficiency measurements on surface-immobilized RNase H, and suggest unfolded state dynamics on time scales from microseconds to seconds.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15471-15476
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 40
    • 33746823043 scopus 로고    scopus 로고
    • Coil-globule transition in the denatured state of a small protein
    • The mean FRET efficiency and hydrodynamic radius from FCS indicate collapse of the unfolded protein L subpopulation upon decreasing denaturant concentration. The collapse is analyzed in terms of a coil-globule transition to obtain information about the solvation properties of the unfolded state.
    • Sherman E., and Haran G. Coil-globule transition in the denatured state of a small protein. Proc Natl Acad Sci U S A 103 (2006) 11539-11543. The mean FRET efficiency and hydrodynamic radius from FCS indicate collapse of the unfolded protein L subpopulation upon decreasing denaturant concentration. The collapse is analyzed in terms of a coil-globule transition to obtain information about the solvation properties of the unfolded state.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11539-11543
    • Sherman, E.1    Haran, G.2
  • 43
    • 0041321045 scopus 로고    scopus 로고
    • Single-molecule measurement of protein folding kinetics
    • Lipman E.A., Schuler B., Bakajin O., and Eaton W.A. Single-molecule measurement of protein folding kinetics. Science 301 (2003) 1233-1235
    • (2003) Science , vol.301 , pp. 1233-1235
    • Lipman, E.A.1    Schuler, B.2    Bakajin, O.3    Eaton, W.A.4
  • 44
    • 34347218159 scopus 로고    scopus 로고
    • Conformational dynamics and ensembles in protein folding
    • Muñoz V. Conformational dynamics and ensembles in protein folding. Annu Rev Biophys Biomol Struct 36 (2007) 395-412
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 395-412
    • Muñoz, V.1
  • 46
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: a synthesis
    • Bryngelson J.D., Onuchic J.N., Socci N.D., and Wolynes P.G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21 (1995) 167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 47
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • The prion-determining NM domain of the yeast prion protein Sup35 is shown to undergo a continuous expansion rather than a cooperative unfolding transition upon addition of denaturant. Fluorescence intensity fluctuations in the submicrosecond range are assigned to chain dynamics resulting in rapid intramolecular quenching by tyrosine.
    • Mukhopadhyay S., Krishnan R., Lemke E.A., Lindquist S., and Deniz A.A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A 104 (2007) 2649-2654. The prion-determining NM domain of the yeast prion protein Sup35 is shown to undergo a continuous expansion rather than a cooperative unfolding transition upon addition of denaturant. Fluorescence intensity fluctuations in the submicrosecond range are assigned to chain dynamics resulting in rapid intramolecular quenching by tyrosine.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 50
    • 0032978994 scopus 로고    scopus 로고
    • Chain collapse can occur concomitantly with the rate-limiting step in protein folding
    • Plaxco K.W., Millett I.S., Segel D.J., Doniach S., and Baker D. Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nat Struct Biol 6 (1999) 554-556
    • (1999) Nat Struct Biol , vol.6 , pp. 554-556
    • Plaxco, K.W.1    Millett, I.S.2    Segel, D.J.3    Doniach, S.4    Baker, D.5
  • 51
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion B.J., and Daggett V. The molecular basis for the chemical denaturation of proteins by urea. Proc Natl Acad Sci U S A 100 (2003) 5142-5147
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 52
    • 33745955427 scopus 로고    scopus 로고
    • Specificity of the initial collapse in the folding of the cold shock protein
    • Magg C., Kubelka J., Holtermann G., Haas E., and Schmid F.X. Specificity of the initial collapse in the folding of the cold shock protein. J Mol Biol 360 (2006) 1067-1080
    • (2006) J Mol Biol , vol.360 , pp. 1067-1080
    • Magg, C.1    Kubelka, J.2    Holtermann, G.3    Haas, E.4    Schmid, F.X.5
  • 54
    • 0036400715 scopus 로고    scopus 로고
    • Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    • Dyson H.J., and Wright P.E. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv Protein Chem 62 (2002) 311-340
    • (2002) Adv Protein Chem , vol.62 , pp. 311-340
    • Dyson, H.J.1    Wright, P.E.2
  • 55
    • 0036401140 scopus 로고    scopus 로고
    • Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins
    • Millett I.S., Doniach S., and Plaxco K.W. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins. Adv Protein Chem 62 (2002) 241-262
    • (2002) Adv Protein Chem , vol.62 , pp. 241-262
    • Millett, I.S.1    Doniach, S.2    Plaxco, K.W.3
  • 56
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi Z., Woody R.W., and Kallenbach N.R. Is polyproline II a major backbone conformation in unfolded proteins?. Adv Protein Chem 62 (2002) 163-240
    • (2002) Adv Protein Chem , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 58
    • 33847254454 scopus 로고    scopus 로고
    • Ultrafast dynamics of protein collapse from single-molecule photon statistics
    • Global chain reconfiguration dynamics on a 50 ns time scale are measured for unfolded CspTm in subpopulation-specific correlation experiments. Increased internal friction causes the dynamics to slow down in the more compact denatured state at low denaturant concentrations. This finding may explain the flat chevron observed for an ultrafast-folding protein [65] and raises the possibility of related effects on the folding kinetics of other proteins.
    • Nettels D., Gopich I.V., Hoffmann A., and Schuler B. Ultrafast dynamics of protein collapse from single-molecule photon statistics. Proc Natl Acad Sci U S A 104 (2007) 2655-2660. Global chain reconfiguration dynamics on a 50 ns time scale are measured for unfolded CspTm in subpopulation-specific correlation experiments. Increased internal friction causes the dynamics to slow down in the more compact denatured state at low denaturant concentrations. This finding may explain the flat chevron observed for an ultrafast-folding protein [65] and raises the possibility of related effects on the folding kinetics of other proteins.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2655-2660
    • Nettels, D.1    Gopich, I.V.2    Hoffmann, A.3    Schuler, B.4
  • 59
    • 0037663777 scopus 로고    scopus 로고
    • Nanosecond dynamics of single polypeptide molecules revealed by photoemission statistics of fluorescence resonance energy transfer: a theoretical study
    • Wang Z.S., and Makarov D.E. Nanosecond dynamics of single polypeptide molecules revealed by photoemission statistics of fluorescence resonance energy transfer: a theoretical study. J Phys Chem B 107 (2003) 5617-5622
    • (2003) J Phys Chem B , vol.107 , pp. 5617-5622
    • Wang, Z.S.1    Makarov, D.E.2
  • 60
    • 34547554494 scopus 로고    scopus 로고
    • Theory of the statistics of kinetic transitions with application to single-molecule enzyme catalysis
    • Gopich I.V., and Szabo A. Theory of the statistics of kinetic transitions with application to single-molecule enzyme catalysis. J Chem Phys 124 (2006) 154712
    • (2006) J Chem Phys , vol.124 , pp. 154712
    • Gopich, I.V.1    Szabo, A.2
  • 61
    • 36749116443 scopus 로고
    • 1st passage time approach to diffusion controlled reactions
    • Szabo A., Schulten K., and Schulten Z. 1st passage time approach to diffusion controlled reactions. J Chem Phys 72 (1980) 4350-4357
    • (1980) J Chem Phys , vol.72 , pp. 4350-4357
    • Szabo, A.1    Schulten, K.2    Schulten, Z.3
  • 62
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci N.D., Onuchic J.N., and Wolynes P.G. Diffusive dynamics of the reaction coordinate for protein folding funnels. J Chem Phys 104 (1996) 5860-5868
    • (1996) J Chem Phys , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 63
    • 33744952224 scopus 로고    scopus 로고
    • Diffusive model of protein folding dynamics with Kramers turnover in rate
    • Best R.B., and Hummer G. Diffusive model of protein folding dynamics with Kramers turnover in rate. Phys Rev Lett 96 (2006) 228104
    • (2006) Phys Rev Lett , vol.96 , pp. 228104
    • Best, R.B.1    Hummer, G.2
  • 64
    • 35548963462 scopus 로고    scopus 로고
    • Configuration-dependent diffusion can shift the kinetic transition state and barrier height of protein folding
    • Chahine J., Oliveira R.J., Leite V.B.P., and Wang J. Configuration-dependent diffusion can shift the kinetic transition state and barrier height of protein folding. Proc Natl Acad Sci U S A 104 (2007) 14646-14651
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14646-14651
    • Chahine, J.1    Oliveira, R.J.2    Leite, V.B.P.3    Wang, J.4
  • 65
    • 36749012371 scopus 로고    scopus 로고
    • Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA: Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration. J Am Chem Soc 2007, 129:14564-14566.
    • Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA: Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration. J Am Chem Soc 2007, 129:14564-14566.
  • 66
    • 0033613165 scopus 로고    scopus 로고
    • A simple model for calculating the kinetics of protein folding from three-dimensional structures
    • Muñoz V., and Eaton W.A. A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc Natl Acad Sci U S A 96 (1999) 11311-11316
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11311-11316
    • Muñoz, V.1    Eaton, W.A.2
  • 67
    • 0242330738 scopus 로고    scopus 로고
    • The importance of explicit chain representation in protein folding models: an examination of Ising-like models
    • Karanicolas J., and Brooks C.L. The importance of explicit chain representation in protein folding models: an examination of Ising-like models. Proteins 53 (2003) 740-747
    • (2003) Proteins , vol.53 , pp. 740-747
    • Karanicolas, J.1    Brooks, C.L.2
  • 68
    • 0034743155 scopus 로고    scopus 로고
    • From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding
    • Shea J.E., and Brooks C.L. From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding. Annu Rev Phys Chem 52 (2001) 499-535
    • (2001) Annu Rev Phys Chem , vol.52 , pp. 499-535
    • Shea, J.E.1    Brooks, C.L.2
  • 70
    • 8844247109 scopus 로고    scopus 로고
    • Two-state folding observed in individual protein molecules
    • Rhoades E., Cohen M., Schuler B., and Haran G. Two-state folding observed in individual protein molecules. J Am Chem Soc 126 (2004) 14686-14687
    • (2004) J Am Chem Soc , vol.126 , pp. 14686-14687
    • Rhoades, E.1    Cohen, M.2    Schuler, B.3    Haran, G.4
  • 71
    • 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., Röcker C., Nienhaus G.U., and Möller M. Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins. J Am Chem Soc 126 (2004) 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    Röcker, C.5    Nienhaus, G.U.6    Möller, M.7
  • 72
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke T.M., and Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat Struct Biol 4 (1997) 298-304
    • (1997) Nat Struct Biol , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 73
    • 0035807849 scopus 로고    scopus 로고
    • Protein folding pathways of adenylate kinase from E. coli: hydrostatic pressure and stopped-flow studies
    • Ruan Q., Ruan K., Balny C., Glaser M., and Mantulin W.W. Protein folding pathways of adenylate kinase from E. coli: hydrostatic pressure and stopped-flow studies. Biochemistry 40 (2001) 14706-14714
    • (2001) Biochemistry , vol.40 , pp. 14706-14714
    • Ruan, Q.1    Ruan, K.2    Balny, C.3    Glaser, M.4    Mantulin, W.W.5
  • 74
    • 33645223271 scopus 로고    scopus 로고
    • Suppressing Brownian motion of individual biomolecules in solution
    • Cohen A.E., and Moerner W.E. Suppressing Brownian motion of individual biomolecules in solution. Proc Natl Acad Sci U S A 103 (2006) 4362-4365
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4362-4365
    • Cohen, A.E.1    Moerner, W.E.2
  • 75
    • 34547512144 scopus 로고    scopus 로고
    • Development of a technique for the investigation of folding dynamics of single proteins for extended time periods
    • Kinoshita M., Kamagata K., Maeda A., Goto Y., Komatsuzaki T., and Takahashi S. Development of a technique for the investigation of folding dynamics of single proteins for extended time periods. Proc Natl Acad Sci U S A 104 (2007) 10453-10458
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10453-10458
    • Kinoshita, M.1    Kamagata, K.2    Maeda, A.3    Goto, Y.4    Komatsuzaki, T.5    Takahashi, S.6
  • 76
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • Hohng S., Joo C., and Ha T. Single-molecule three-color FRET. Biophys J 87 (2004) 1328-1337
    • (2004) Biophys J , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 77
    • 13444291091 scopus 로고    scopus 로고
    • Three-color single-molecule fluorescence resonance energy transfer
    • Clamme J.P., and Deniz A.A. Three-color single-molecule fluorescence resonance energy transfer. Chemphyschem 6 (2005) 74-77
    • (2005) Chemphyschem , vol.6 , pp. 74-77
    • Clamme, J.P.1    Deniz, A.A.2
  • 78
    • 33846028172 scopus 로고    scopus 로고
    • Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances
    • Lee N.K., Kapanidis A.N., Koh H.R., Korlann Y., Ho S.O., Kim Y., Gassman N., Kim S.K., and Weiss S. Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances. Biophys J 92 (2007) 303-312
    • (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
  • 79
    • 0037461520 scopus 로고    scopus 로고
    • Fluorescent probes and bioconjugation chemistries for single-molecule fluorescence analysis of biomolecules
    • Kapanidis A.N., and Weiss S. Fluorescent probes and bioconjugation chemistries for single-molecule fluorescence analysis of biomolecules. J Chem Phys 117 (2002) 10953-10964
    • (2002) J Chem Phys , vol.117 , pp. 10953-10964
    • Kapanidis, A.N.1    Weiss, S.2
  • 80
    • 0033437006 scopus 로고    scopus 로고
    • Analyzing single molecule trajectories on complex energy landscapes using replica correlation functions
    • Onuchic J.N., Wang J., and Wolynes P.G. Analyzing single molecule trajectories on complex energy landscapes using replica correlation functions. Chem Phys 247 (1999) 175-184
    • (1999) Chem Phys , vol.247 , pp. 175-184
    • Onuchic, J.N.1    Wang, J.2    Wolynes, P.G.3
  • 81
    • 2442482377 scopus 로고    scopus 로고
    • GroEL mediates protein folding with a two successive timer mechanism
    • Ueno T., Taguchi H., Tadakuma H., Yoshida M., and Funatsu T. GroEL mediates protein folding with a two successive timer mechanism. Mol Cell 14 (2004) 423-434
    • (2004) Mol Cell , vol.14 , pp. 423-434
    • Ueno, T.1    Taguchi, H.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 83
    • 35948935175 scopus 로고    scopus 로고
    • Hillger F, Nettels D, Dorsch S, Schuler B: Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy. J Fluoresc 2007, 17:759-765.
    • Hillger F, Nettels D, Dorsch S, Schuler B: Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy. J Fluoresc 2007, 17:759-765.
  • 84
    • 3042631531 scopus 로고    scopus 로고
    • Time-resolved confocal fluorescence imaging and spectroscopy system with single molecule sensitivity and sub-micrometer resolution
    • Wahl M., Koberling F., Patting M., Rahn H., and Erdmann R. Time-resolved confocal fluorescence imaging and spectroscopy system with single molecule sensitivity and sub-micrometer resolution. Curr Pharm Biotechnol 5 (2004) 299-308
    • (2004) Curr Pharm Biotechnol , vol.5 , pp. 299-308
    • Wahl, M.1    Koberling, F.2    Patting, M.3    Rahn, H.4    Erdmann, R.5


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