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Volumn 502, Issue 7473, 2013, Pages 685-688

Single-molecule fluorescence probes dynamics of barrier crossing

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; SOLVENT;

EID: 84886954019     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12649     Document Type: Article
Times cited : (214)

References (38)
  • 1
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H. A. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7, 284-304 (1940)
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 2
    • 0347193736 scopus 로고
    • Reaction rate theory; Fifty years after Kramers
    • Hänggi, P., Talkner, P. & Borkovec, M. Reaction rate theory; fifty years after Kramers. Rev. Mod. Phys. 62, 251-341 (1990)
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 251-341
    • Hänggi, P.1    Talkner, P.2    Borkovec, M.3
  • 3
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • Oliveberg, M. & Wolynes, P. G. The experimental survey of protein-folding energy landscapes. Q. Rev. Biophys. 38, 245-288 (2005)
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 5
    • 84857510185 scopus 로고    scopus 로고
    • Single-molecule fluorescence experiments determine protein folding transition path times
    • Chung, H. S., McHale, K., Louis, J. M. & Eaton, W. A. Single-molecule fluorescence experiments determine protein folding transition path times. Science 335, 981-984 (2012)
    • (2012) Science , vol.335 , pp. 981-984
    • Chung, H.S.1    McHale, K.2    Louis, J.M.3    Eaton, W.A.4
  • 6
    • 78649562607 scopus 로고    scopus 로고
    • Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein
    • Chung, H. S. et al. Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein. J. Phys. Chem. A 115, 3642-3656 (2011)
    • (2011) J. Phys. Chem. A , vol.115 , pp. 3642-3656
    • Chung, H.S.1
  • 8
    • 68149166290 scopus 로고    scopus 로고
    • Decoding the pattern of photon colors in single-molecule FRET
    • Gopich, I. V. & Szabo, A. Decoding the pattern of photon colors in single-molecule FRET. J. Phys. Chem. B 113, 10965-10973 (2009)
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10965-10973
    • Gopich, I.V.1    Szabo, A.2
  • 9
    • 67749147584 scopus 로고    scopus 로고
    • Experimental determinationofupper bound for transition path times in protein folding from single-molecule photon-byphoton trajectories
    • Chung, H. S., Louis, J. M. &Eaton, W. A. Experimental determinationofupper bound for transition path times in protein folding from single-molecule photon-byphoton trajectories. Proc. Natl Acad. Sci. USA 106, 11837-11844 (2009)
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11837-11844
    • Chung, H.S.1    Louis, J.M.2    Eaton, W.A.3
  • 10
    • 84885621197 scopus 로고    scopus 로고
    • Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories
    • Chung, H. S., Cellmer, T., Louis, J. M. & Eaton, W. A. Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories. Chem. Phys. 422, 229-237 (2013)
    • (2013) Chem. Phys. , vol.422 , pp. 229-237
    • Chung, H.S.1    Cellmer, T.2    Louis, J.M.3    Eaton, W.A.4
  • 11
    • 0842311640 scopus 로고    scopus 로고
    • From transition paths to transition states and rate coefficients
    • Hummer, G. From transition paths to transition states and rate coefficients. J. Chem. Phys. 120, 516-523 (2004)
    • (2004) J. Chem. Phys. , vol.120 , pp. 516-523
    • Hummer, G.1
  • 12
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N. D., Onuchic, J. N. & Wolynes, P. G. Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104, 5860-5868 (1996)
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 13
    • 0000399469 scopus 로고    scopus 로고
    • Viscosity dependence of the folding rates of proteins
    • Klimov, D. K. &Thirumalai, D. Viscosity dependence of the folding rates of proteins. Phys. Rev. Lett. 79, 317-320 (1997)
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 317-320
    • Klimov, D.K.1    Thirumalai, D.2
  • 14
    • 18744387720 scopus 로고    scopus 로고
    • Reaction coordinates and rates from transition paths
    • Best, R. B. & Hummer, G. Reaction coordinates and rates from transition paths. Proc. Natl Acad. Sci. USA 102, 6732-6737 (2005)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6732-6737
    • Best, R.B.1    Hummer, G.2
  • 17
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. &Gruebele, M. Folding at the speed limit. Nature423,193-197 (2003)
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 18
    • 23744478437 scopus 로고    scopus 로고
    • Free energy surfaces from single-molecule force spectroscopy
    • Hummer, G. & Szabo, A. Free energy surfaces from single-molecule force spectroscopy. Acc. Chem. Res. 38, 504-513 (2005)
    • (2005) Acc. Chem. Res. , vol.38 , pp. 504-513
    • Hummer, G.1    Szabo, A.2
  • 19
    • 44949236102 scopus 로고    scopus 로고
    • Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data
    • Godoy-Ruiz, R. et al. Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. J. Phys. Chem. B 112, 5938-5949 (2008)
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5938-5949
    • Godoy-Ruiz, R.1
  • 20
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates II. Local reaction coordinates and chain dynamics
    • Portman, J. J., Takada, S. & Wolynes, P. G. Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics. J. Chem. Phys. 114, 5082-5096 (2001)
    • (2001) J. Chem. Phys. , vol.114 , pp. 5082-5096
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 21
    • 84872066560 scopus 로고    scopus 로고
    • Interplay of non-Markov and internal friction effects in the barrier crossing kinetics of biopolymers: Insights from an analytically solvable model
    • Makarov, D. E. Interplay of non-Markov and internal friction effects in the barrier crossing kinetics of biopolymers: insights from an analytically solvable model. J. Chem. Phys. 138, 014102 (2013)
    • (2013) J. Chem. Phys. , vol.138 , pp. 014102
    • Makarov, D.E.1
  • 22
    • 84859565600 scopus 로고    scopus 로고
    • Peptide chain dynamics in light and heavy water: Zooming in on internal friction
    • Schulz, J. C. F., Schmidt, L., Best, R. B., Dzubiella, J. & Netz, R. R. Peptide chain dynamics in light and heavy water: zooming in on internal friction. J. Am. Chem. Soc. 134, 6273-6279 (2012)
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6273-6279
    • Schulz, J.C.F.1    Schmidt, L.2    Best, R.B.3    Dzubiella, J.4    Netz, R.R.5
  • 23
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J. & Eaton, W. A. The role of solvent viscosity in the dynamics of protein conformational changes. Science 256, 1796-1798 (1992)
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 24
    • 84862076708 scopus 로고    scopus 로고
    • Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy
    • Soranno, A. et al. Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. Proc. Natl Acad. Sci. USA 109, 17800-17806 (2012)
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 17800-17806
    • Soranno, A.1
  • 25
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy-model (with applications to protein folding
    • Bryngelson, J. D. & Wolynes, P. G. Intermediates and barrier crossing in a random energy-model (with applications to protein folding). J. Phys. Chem. 93, 6902-6915 (1989)
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 26
    • 0042561888 scopus 로고    scopus 로고
    • Solvent viscosity dependence of the folding rate of a small protein: Distributed computing study
    • Zagrovic, B. & Pande, V. Solvent viscosity dependence of the folding rate of a small protein: distributed computing study. J. Comput. Chem. 24, 1432-1436 (2003)
    • (2003) J. Comput. Chem. , vol.24 , pp. 1432-1436
    • Zagrovic, B.1    Pande, V.2
  • 27
    • 38049140954 scopus 로고    scopus 로고
    • Consequences of localized frustration for the folding mechanismof the IM7 protein
    • Sutto, L., Latzer, J., Hegler, J. A., Ferreiro, D. U. & Wolynes, P. G. Consequences of localized frustration for the folding mechanismof the IM7 protein. Proc. Natl Acad. Sci. USA 104, 19825-19830 (2007)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19825-19830
    • Sutto, L.1    Latzer, J.2    Hegler, J.A.3    Ferreiro, D.U.4    Wolynes, P.G.5
  • 28
    • 0035128362 scopus 로고    scopus 로고
    • Effect of viscosity on the kinetics of a-helix and b-hairpin formation
    • Jas, G. S., Eaton, W. A. &Hofrichter, J. Effect of viscosity on the kinetics of a-helix and b-hairpin formation. J. Phys. Chem. B 105, 261-272 (2001)
    • (2001) J. Phys. Chem. B , vol.105 , pp. 261-272
    • Jas, G.S.1    Eaton, W.A.2    Hofrichter, J.3
  • 29
    • 76249117417 scopus 로고    scopus 로고
    • Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family
    • Wensley, B. G. et al. Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family. Nature 463, 685-688 (2010)
    • (2010) Nature , vol.463 , pp. 685-688
    • Wensley, B.G.1
  • 30
    • 77957916566 scopus 로고    scopus 로고
    • Solvent viscosity and friction in protein folding dynamics
    • Hagen, S. J. Solvent viscosity and friction in protein folding dynamics. Curr. Protein Pept. Sci. 11, 385-395 (2010)
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 385-395
    • Hagen, S.J.1
  • 31
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • Merchant, K. A., Best, R. B., Louis, J. M., Gopich, I. V. & Eaton, W. A. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc. Natl Acad. Sci. USA 104, 1528-1533 (2007)
    • (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
  • 32
    • 53549084075 scopus 로고    scopus 로고
    • A reducing and oxidizing system minimizes photobleaching and blinking of fluorescent dyes
    • Vogelsang, J. et al. A reducing and oxidizing system minimizes photobleaching and blinking of fluorescent dyes. Angew. Chem. 47, 5465-5469 (2008)
    • (2008) Angew. Chem. , vol.47 , pp. 5465-5469
    • Vogelsang, J.1
  • 33
    • 33645694727 scopus 로고    scopus 로고
    • Quantitative 3D mapping of fluidic temperatures within microchannel networks using fluorescence lifetime imaging
    • Benninger, R. K. P. et al. Quantitative 3D mapping of fluidic temperatures within microchannel networks using fluorescence lifetime imaging. Anal. Chem. 78, 2272-2278 (2006)
    • (2006) Anal. Chem. , vol.78 , pp. 2272-2278
    • Benninger, R.K.P.1
  • 34
    • 84935113569 scopus 로고
    • Error bounds for convolution codes and an asymptotically optimum decoding algorithm
    • Viterbi, A. J. Error bounds for convolution codes and an asymptotically optimum decoding algorithm. IEEE Trans. Inf. Theory 13, 260-269 (1967)
    • (1967) IEEE Trans. Inf. Theory , vol.13 , pp. 260-269
    • Viterbi, A.J.1
  • 35
    • 0024610919 scopus 로고
    • A tutorial on hidden Markov models and selected applications in speech
    • Rabiner, L. R. A tutorial on hidden Markov models and selected applications in speech. Proc. IEEE 77, 257-286 (1989)
    • (1989) Proc. IEEE , vol.77 , pp. 257-286
    • Rabiner, L.R.1
  • 36
    • 84887117718 scopus 로고    scopus 로고
    • Native contacts determine protein folding mechanisms in atomistic simulations
    • in the press
    • Best, R. B., Hummer, G. & Eaton, W. A. Native contacts determine protein folding mechanisms in atomistic simulations. Proc. Natl Acad. Sci USA. http://dx. doi. org/
    • Proc. Natl Acad. Sci USA.
    • Best, R.B.1    Hummer, G.2    Eaton, W.A.3
  • 37
    • 0346734133 scopus 로고    scopus 로고
    • Ultrafast folding of a3D: A de novo designed three-helix bundle protein
    • Zhu, Y. et al. Ultrafast folding of a3D: a de novo designed three-helix bundle protein. Proc. Natl Acad. Sci. USA 100, 15486-15491 (2003)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15486-15491
    • Zhu, Y.1
  • 38
    • 60349085890 scopus 로고    scopus 로고
    • A one-dimensional free energy surface does not account for twoprobe folding kinetics of protein a3D
    • Liu, F. et al. A one-dimensional free energy surface does not account for twoprobe folding kinetics of protein a3D. J. Chem. Phys. 130, 061101 (2009)
    • (2009) J. Chem. Phys. , vol.130 , pp. 061101
    • Liu, F.1


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