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Volumn 99, Issue 2, 2010, Pages 600-608

The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN;

EID: 77955200083     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.04.041     Document Type: Article
Times cited : (33)

References (82)
  • 1
    • 0026723063 scopus 로고
    • Protein folding funnels - A kinetic approach to the sequence structure relationship
    • Leopold, P. E., M. Montai, and J. N. Onuchic. 1992. Protein folding funnels - a kinetic approach to the sequence structure relationship. Proc. Natl. Acad. Sci. USA. 18: 8721-8725.
    • (1992) Proc. Natl. Acad. Sci. USA. , vol.18 , pp. 8721-8725
    • Leopold, P.E.1    Montai, M.2    Onuchic, J.N.3
  • 2
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., J. N. Onuchic, ..., P. G. Wolynes. 1995. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins. 21: 167-195.
    • (1995) Proteins. , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 3
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J. D., and P. G. Wolynes. 1987. Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA. 84: 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. USA. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 5
    • 0001209011 scopus 로고    scopus 로고
    • Statistics of kinetic pathways on biased rough energy landscapes with applications to protein folding
    • Wang, J., J. N. Onuchic, and P. G. Wolynes. 1996. Statistics of kinetic pathways on biased rough energy landscapes with applications to protein folding. Phys. Rev. Lett. 76: 4861-4864. (Pubitemid 126640475)
    • (1996) Physical Review Letters , vol.76 , Issue.25 , pp. 4861-4864
    • Wang, J.1    Onuchic, J.2    Wolynes, P.3
  • 8
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • Clementi, C., H. Nymeyer, and J. N. Onuchic. 2000. Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins. J. Mol. Biol. 298: 937-953.
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 9
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1 β
    • Gosavi, S., L. L. Chavez, ..., J. N. Onuchic. 2006. Topological frustration and the folding of interleukin-1 β. J. Mol. Biol. 357: 986-996.
    • (2006) J. Mol. Biol. , vol.357 , pp. 986-996
    • Gosavi, S.1    Chavez, L.L.2    Onuchic, J.N.3
  • 10
    • 63449135082 scopus 로고    scopus 로고
    • An all-atom structure-based potential for proteins: Bridging minimal models with allatom empirical forcefields
    • Whitford, P. C., J. K. Noel, ..., J. N. Onuchic. 2009. An all-atom structure-based potential for proteins: bridging minimal models with allatom empirical forcefields. Proteins Struct. Funct. Bioinf 75: 430-441.
    • (2009) Proteins Struct. Funct. Bioinf , vol.75 , pp. 430-441
    • Whitford, P.C.1    Noel, J.K.2    Onuchic, J.N.3
  • 11
    • 33644986099 scopus 로고    scopus 로고
    • Mechanisms of protein assembly: Lessons from minimalist models
    • Levy, Y., and J. N. Onuchic. 2006. Mechanisms of protein assembly: lessons from minimalist models. Acc. Chem. Res. 39: 135-142.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 135-142
    • Levy, Y.1    Onuchic, J.N.2
  • 12
    • 4644301408 scopus 로고    scopus 로고
    • Domain swapping is a consequence of minimal frustration
    • Yang, S. C., S. S. Cho, ..., J. N. Onuchic. 2004. Domain swapping is a consequence of minimal frustration. Proc. Natl. Acad. Sci. USA. 101: 13786-13791.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 13786-13791
    • Yang, S.C.1    Cho, S.S.2    Onuchic, J.N.3
  • 13
    • 33947586778 scopus 로고    scopus 로고
    • Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
    • DOI 10.1103/PhysRevLett.98.128105
    • Lu, Q., H. P. Lu, and J. Wang. 2007. Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics. Phys. Rev. Lett. 98: 128105. (Pubitemid 46476755)
    • (2007) Physical Review Letters , vol.98 , Issue.12 , pp. 128105
    • Lu, Q.1    Lu, H.P.2    Wang, J.3
  • 14
    • 33846847773 scopus 로고    scopus 로고
    • Conformational transitions of adenylate kinase: Switching by cracking
    • Whitford, P. C., O. Miyashita, ..., J. N. Onuchic. 2007. Conformational transitions of adenylate kinase: switching by cracking. J. Mol. Biol. 366: 1661-1671.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1661-1671
    • Whitford, P.C.1    Miyashita, O.2    Onuchic, J.N.3
  • 16
    • 28844466824 scopus 로고    scopus 로고
    • Slow protein conformational dynamics from multiple experimental structures: The helix/sheet transition of arc repressor
    • Best, R. B., Y. G. Chen, and G. Hummer. 2005. Slow protein conformational dynamics from multiple experimental structures: the helix/sheet transition of arc repressor. Structure. 13: 1755-1763.
    • (2005) Structure. , vol.13 , pp. 1755-1763
    • Best, R.B.1    Chen, Y.G.2    Hummer, G.3
  • 17
    • 2342471328 scopus 로고    scopus 로고
    • Simulation of an ensemble of conformational transitions in a united-residue model of calmodulin
    • Zuckerman, D. M. 2004. Simulation of an ensemble of conformational transitions in a united-residue model of calmodulin, J. Phys. Chem. B. 108: 5127-5137.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 5127-5137
    • Zuckerman, D.M.1
  • 18
    • 41849107614 scopus 로고    scopus 로고
    • Single molecule conformational dynamics of adenylate kinase: Energy landscape, structural correlations, and transition state ensembles
    • DOI 10.1021/ja0780481
    • Lu, Q., and J. Wang. 2008. Single molecule conformational dynamics of adenylate kinase: energy landscape, structural correlations, and transition state ensembles. J. Am. Chem. Soc. 130: 4772-4783. (Pubitemid 351500112)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.14 , pp. 4772-4783
    • Lu, Q.1    Wang, J.2
  • 19
    • 58049211534 scopus 로고    scopus 로고
    • Minimal models for proteins and RNA: From folding to function
    • Progress in Molecular Biology and Translational Science.. Elsevier/Academic Press, Amsterdam, The Netherlands
    • Pincus, D. L., S. S. Cho, ..., D. Thirumalai. 2008. Minimal models for proteins and RNA: from folding to function. In Molecular Biology of Protein Folding, Pt B, Vol. 84, Progress in Molecular Biology and Translational Science.. Elsevier/Academic Press, Amsterdam, The Netherlands.
    • (2008) Molecular Biology of Protein Folding, Pt B , vol.84
    • Pincus, D.L.1    Cho, S.S.2    Thirumalai, D.3
  • 20
    • 38049119865 scopus 로고    scopus 로고
    • Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations
    • Mickler, M., R. I. Dima, ..., M. Rief. 2007. Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations. Proc. Natl. Acad. Sci. USA. 104: 20268-20273.
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 20268-20273
    • Mickler, M.1    Dima, R.I.2    Rief, M.3
  • 21
    • 63449129633 scopus 로고    scopus 로고
    • Insights from coarsegrained Go models for protein folding and dynamics
    • Hills, Jr., R. D., and C. L. Brooks, III. 2009. Insights from coarsegrained Go models for protein folding and dynamics. Int. J. Mol. Sci. 10: 889-905.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 889-905
    • Hills Jr., R.D.1    Brooks III, C.L.2
  • 22
    • 0242383943 scopus 로고    scopus 로고
    • Improved Gō-like models demonstrate the robustness of protein folding mechanisms towards non-native interactions
    • DOI 10.1016/j.jmb.2003.09.047
    • Karanicolas, J., and C. L. Brooks, 3rd. 2003. Improved Gō-like models demonstrate the robustness of protein folding mechanisms towards nonnative interactions. J. Mol. Biol. 334: 309-325. (Pubitemid 37357269)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.2 , pp. 309-325
    • Karanicolas, J.1    Brooks III, C.L.2
  • 23
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effects of specific amino acid sequence represented by specific inter-unit interactions
    • Ueda, Y., H. Taketomi, and N. Go. 1975. Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effects of specific amino acid sequence represented by specific inter-unit interactions. Int. J. Peptide Res. 7: 445-459.
    • (1975) Int. J. Peptide Res. , vol.7 , pp. 445-459
    • Ueda, Y.1    Taketomi, H.2    Go, N.3
  • 24
    • 3142782241 scopus 로고    scopus 로고
    • Quantifying the roughness on the free energy landscape: Entropic bottlenecks and protein folding rates
    • Chavez, L. L., J. N. Onuchic, and C. Clementi. 2004. Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates. J. Am. Chem. Soc. 126: 8426-8432.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8426-8432
    • Chavez, L.L.1    Onuchic, J.N.2    Clementi, C.3
  • 25
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N. D., J. N. Onuchic, and P. G. Wolynes. 1996. Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104: 5860-5868.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 26
    • 41349108451 scopus 로고    scopus 로고
    • Diffusive dynamics of protein folding studied by molecular dynamics simulations of an off-lattice model
    • Baumketner, A., and Y. Hiwatari. 2002. Diffusive dynamics of protein folding studied by molecular dynamics simulations of an off-lattice model. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 66: 011905.
    • (2002) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.66 , pp. 011905
    • Baumketner, A.1    Hiwatari, Y.2
  • 27
    • 0030628053 scopus 로고    scopus 로고
    • On the theory of folding kinetics for short proteins
    • Pande, V. S., A. Y. Grosberg, and T. Tanaka. 1997. On the theory of folding kinetics for short proteins. Fold. Des. 2: 109-114.
    • (1997) Fold. Des. , vol.2 , pp. 109-114
    • Pande, V.S.1    Grosberg, A.Y.2    Tanaka, T.3
  • 28
    • 0001563395 scopus 로고    scopus 로고
    • On the transition coordinate for protein folding
    • Du, R., V. S. Pande, ..., E. S. Shakhnovich. 1998. On the transition coordinate for protein folding. J. Chem. Phys. 108: 334-350.
    • (1998) J. Chem. Phys. , vol.108 , pp. 334-350
    • Du, R.1    Pande, V.S.2    Shakhnovich, E.S.3
  • 30
    • 0037425662 scopus 로고    scopus 로고
    • First-passage time distribution and non-Markovian diffusion dynamics of protein folding
    • Lee, C. L., G. Stell, and J. Wang. 2003. First-passage time distribution and non-Markovian diffusion dynamics of protein folding. J. Chem. Phys. 118: 959-968.
    • (2003) J. Chem. Phys. , vol.118 , pp. 959-968
    • Lee, C.L.1    Stell, G.2    Wang, J.3
  • 31
    • 85003318612 scopus 로고    scopus 로고
    • Diffusion dynamics, moments, and distribution of first-passage time on the protein-folding energy landscape, with applications to single molecules
    • Lee, C. L., C. T. Lin, ..., J. Wang. 2003. Diffusion dynamics, moments, and distribution of first-passage time on the protein-folding energy landscape, with applications to single molecules. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 67: 041905.
    • (2003) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.67 , pp. 041905
    • Lee, C.L.1    Lin, C.T.2    Wang, J.3
  • 33
    • 33746868878 scopus 로고    scopus 로고
    • Effective stochastic dynamics on a protein folding energy landscape
    • Yang, S., J. N. Onuchic, and H. Levine. 2006. Effective stochastic dynamics on a protein folding energy landscape. J. Chem. Phys. 125: 054910-054918.
    • (2006) J. Chem. Phys. , vol.125 , pp. 54910-54918
    • Yang, S.1    Onuchic, J.N.2    Levine, H.3
  • 34
    • 34548273698 scopus 로고    scopus 로고
    • Folding time predictions from all-atom replica exchange simulations
    • DOI 10.1016/j.jmb.2007.07.010, PII S0022283607009242
    • Yang, S., J. N. Onuchic, ..., H. Levine. 2007. Folding time predictions from all-atom replica exchange simulations. J. Mol. Biol. 372: 756-763. (Pubitemid 47321796)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 756-763
    • Yang, S.1    Onuchic, J.N.2    Garcia, A.E.3    Levine, H.4
  • 35
    • 31444452031 scopus 로고    scopus 로고
    • P versus Q: Structural reaction coordinates capture protein folding on smooth landscapes
    • Cho, S. S., Y. Levy, and P. G. Wolynes. 2006. P versus Q: structural reaction coordinates capture protein folding on smooth landscapes. Proc. Natl. Acad. Sci. USA. 103: 586-591.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 586-591
    • Cho, S.S.1    Levy, Y.2    Wolynes, P.G.3
  • 39
    • 44949240469 scopus 로고    scopus 로고
    • Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds
    • Nettels, D., I. V. Gopich, ..., B. Schuler. 2008. Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds. J. Phys. Chem. 112: 6137-6146.
    • (2008) J. Phys. Chem. , vol.112 , pp. 6137-6146
    • Nettels, D.1    Gopich, I.V.2    Schuler, B.3
  • 40
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • Karplus, M., and D. L. Weaver. 1994. Protein folding dynamics: the diffusion-collision model and experimental data. Protein Sci. 3: 650-668. (Pubitemid 24136370)
    • (1994) Protein Science , vol.3 , Issue.4 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 42
    • 23944522022 scopus 로고    scopus 로고
    • Downhill protein folding: Evolution meets physics
    • DOI 10.1016/j.crvi.2005.02.007, PII S1631069105000326
    • Gruebele, M. 2005. Downhill protein folding: evolution meets physics. C. R. Biol. 328: 701-712. (Pubitemid 41200378)
    • (2005) Comptes Rendus - Biologies , vol.328 , Issue.8 , pp. 701-712
    • Gruebele, M.1
  • 43
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random, energy-model (with applications to protein folding)
    • Bryngelson, J. D., and P. G. Wolynes. 1989. Intermediates and barrier crossing in a random, energy-model (with applications to protein folding). J. Phys. Chem. 93: 6902-6915.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 45
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • DOI 10.1017/S0033583506004185, PII S0033583506004185
    • Oliveberg, M., and P. G. Wolynes. 2005. The experimental survey of protein-folding energy landscapes. Q. Rev. Biophys. 38: 245-288. (Pubitemid 44268537)
    • (2005) Quarterly Reviews of Biophysics , vol.38 , Issue.3 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 46
    • 23244438863 scopus 로고    scopus 로고
    • Position-dependent diffusion coefficients and free energies from Bayesian analysis of equilibrium and replica molecular dynamics simulations
    • Hummer, G. 2005. Position-dependent diffusion coefficients and free energies from Bayesian analysis of equilibrium and replica molecular dynamics simulations. N. J. Phys. 7: 34-48.
    • (2005) N. J. Phys. , vol.7 , pp. 34-48
    • Hummer, G.1
  • 47
    • 75749153687 scopus 로고    scopus 로고
    • Coordinate-dependent diffusion in protein folding
    • Best, R. B., and G. Hummer. 2010. Coordinate-dependent diffusion in protein folding. Proc. Natl. Acad. Sci. USA. 107: 1088-1093.
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 1088-1093
    • Best, R.B.1    Hummer, G.2
  • 48
    • 73949104409 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins
    • Nettels, D., S. Mudie;ller-Späth, ..., B. Schuler. 2009. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. Proc. Natl. Acad. Sci. USA. 106: 20740-20745.
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 20740-20745
    • Nettels, D.1    Mudie2    ller-Späth, S.3    Schuler, B.4
  • 49
    • 52949137003 scopus 로고    scopus 로고
    • Diffusive reaction dynamics on invariant free energy profiles
    • Krivov, S. V., and M. Karplus. 2008. Diffusive reaction dynamics on invariant free energy profiles. Proc. Natl. Acad. Sci. USA. 105: 13841-13846.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 13841-13846
    • Krivov, S.V.1    Karplus, M.2
  • 51
    • 0033612222 scopus 로고    scopus 로고
    • Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima
    • Wassenberg, D., C. Welker, and R. Jaenicke. 1999. Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. J. Mol. Biol. 289: 187-193.
    • (1999) J. Mol. Biol. , vol.289 , pp. 187-193
    • Wassenberg, D.1    Welker, C.2    Jaenicke, R.3
  • 53
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • Schuler, B., E. A. Lipman, and W. A. Eaton. 2002. Probing the freeenergy surface for protein folding with single-molecule fluorescence spectroscopy. Nature. 429: 743-747. (Pubitemid 35177962)
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 55
    • 0342929614 scopus 로고
    • Nonphysical sampling distributions in Monte Carlo free-energy estimation - Umbrella sampling
    • Torrie, G. M., and J. P. Valleau. 1977. Nonphysical sampling distributions in Monte Carlo free-energy estimation - umbrella sampling. J. Comput. Phys. 23: 187-199.
    • (1977) J. Comput. Phys. , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 56
    • 4344606960 scopus 로고    scopus 로고
    • Multidimensional adaptive umbrella sampling: Applications to main chain and side chain peptide conformations
    • Bartels, C., and M. Karplus. 1997. Multidimensional adaptive umbrella sampling: applications to main chain and side chain peptide confonnations. J. Comput. Phys. 18: 1450-1462. (Pubitemid 127637343)
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.12 , pp. 1450-1462
    • Bartels, C.1    Karplus, M.2
  • 57
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • DOI 10.1038/340122a0
    • Matouschek, A., J. T. Kellis, Jr, ..., A. R. Fersht. 1989. Mapping the transition state and pathway of protein folding by protein engineering. Nature. 340: 122-126. (Pubitemid 19175363)
    • (1989) Nature , vol.340 , Issue.6229 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 58
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A. R. 1995. Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5: 79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 59
    • 0034681133 scopus 로고    scopus 로고
    • Landscape approaches for determining the ensemble of folding transition states: Success and failure hinge on the degree of frustration
    • DOI 10.1073/pnas.97.2.634
    • Nymeyer, H., N. D. Socci, and J. N. Onuchic. 2000. Landscape approaches for determining the ensemble of folding transition states: success and failure hinge on the degree of frustration. Proc. Natl. Acad. Sci. USA. 97: 634-639. (Pubitemid 30070361)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.2 , pp. 634-639
    • Nymeyer, H.1    Socci, N.D.2    Onuchic, J.N.3
  • 61
    • 85031339989 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 62
    • 0035576033 scopus 로고    scopus 로고
    • Speeding protein folding beyond the Gō model: How a little frustration sometimes helps
    • Plotkin, S. S. 2001. Speeding protein folding beyond the Gō model: how a little frustration sometimes helps. Proteins Struct. Funct. Genet. 45: 337-345.
    • (2001) Proteins Struct. Funct. Genet. , vol.45 , pp. 337-345
    • Plotkin, S.S.1
  • 63
    • 3042677501 scopus 로고    scopus 로고
    • The effects of nonnative interactions on protein folding rates: Theory and simulation
    • DOI 10.1110/ps.03580104
    • Clementi, C., and S. S. Plotkin. 2004. The effects of nonnative interactions on protein folding rates: theory and simulation. Protein Sci. 13: 1750-1766. (Pubitemid 38822115)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1750-1766
    • Clementi, C.1    Plotkin, S.S.2
  • 64
    • 0043094427 scopus 로고    scopus 로고
    • Folding of lattice protein chains with modified Gō potential
    • DOI 10.1140/epjb/e2002-00393-4
    • Fan, K., J. Wang, and W. Wang. 2002. Folding of lattice protein chains with modified Gō potential. Eur. Phys. J. B. 30: 381-391. (Pubitemid 135695550)
    • (2002) European Physical Journal B , vol.30 , Issue.3 , pp. 381-391
    • Fan, K.1    Wang, J.2    Wang, W.3
  • 65
    • 0034112774 scopus 로고    scopus 로고
    • Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus
    • DOI 10.1038/74111
    • Li, L., L. A. Mirny, and E. I. Shakhnovich. 2000. Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus. Nature. 7: 336-342. (Pubitemid 30194459)
    • (2000) Nature Structural Biology , vol.7 , Issue.4 , pp. 336-342
    • Li, L.1    Mirny, L.A.2    Shakhnovich, E.I.3
  • 66
    • 0036836534 scopus 로고    scopus 로고
    • Nonnative interactions, effective contact order, and protein folding: A mutational investigation with the energetically frustrated hydrophobic model
    • Treptow, W. L., M. A. A. Barbosa, ..., A. F. P. de Araújo. 2002. Nonnative interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model. Proteins Struct. Funct. Bioinf. 49: 167-180.
    • (2002) Proteins Struct. Funct. Bioinf. , vol.49 , pp. 167-180
    • Treptow, W.L.1    Barbosa, M.A.A.2    De Araújo, A.F.P.3
  • 67
    • 30344481686 scopus 로고    scopus 로고
    • Folding pathway dependence on energetic frustration and interaction heterogeneity for a three-dimensional hydrophobic protein model
    • Garcia, L. G., and A. F. P. de Araújo. 2006. Folding pathway dependence on energetic frustration and interaction heterogeneity for a three-dimensional hydrophobic protein model. Proteins Struct. Funct. Bioinf. 62: 46-63.
    • (2006) Proteins Struct. Funct. Bioinf. , vol.62 , pp. 46-63
    • Garcia, L.G.1    De Araújo, A.F.P.2
  • 68
    • 34447261443 scopus 로고    scopus 로고
    • The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9
    • Morton, V. L., C. T. Friel, ..., S. E. Radford. 2007. The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9. J. Mol. Biol. 371: 554-568.
    • (2007) J. Mol. Biol. , vol.371 , pp. 554-568
    • Morton, V.L.1    Friel, C.T.2    Radford, S.E.3
  • 69
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
    • DOI 10.1006/jmbi.1997.1055
    • Hamada, D., and Y. Goto. 1997. The equilibrium intermediate of β-lactoglobulin with non-native a-helical structure. J. Mol. Biol. 269: 479-487. (Pubitemid 27267862)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.4 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 71
    • 2542619154 scopus 로고    scopus 로고
    • Dramatic acceleration of protein folding by stabilization of a normative backbone conformation
    • Di Nardo, A. A., D. M. Korzhnev, ..., A. R. Davidson. 2004. Dramatic acceleration of protein folding by stabilization of a normative backbone conformation. Proc. Natl. Acad. Sci. USA. 101: 7954-7959.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 7954-7959
    • Di Nardo, A.A.1    Korzhnev, D.M.2    Davidson, A.R.3
  • 72
    • 33750004434 scopus 로고    scopus 로고
    • Identification of a Collapsed Intermediate with Non-native Long-range Interactions on the Folding Pathway of a Pair of Fyn SH3 Domain Mutants by NMR Relaxation Dispersion Spectroscopy
    • DOI 10.1016/j.jmb.2006.08.047, PII S002228360601076X
    • Neudecker, P., A. Zarrine-Afsar, ..., L. E. Kay. 2006. Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy. J. Mol. Biol. 363: 958-976. (Pubitemid 44573226)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.5 , pp. 958-976
    • Neudecker, P.1    Zarrine-Afsar, A.2    Choy, W.-Y.3    Muhandiram, D.R.4    Davidson, A.R.5    Kay, L.E.6
  • 73
    • 66749176784 scopus 로고    scopus 로고
    • The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure
    • Shan, B., D. Eliezer, and D. P. Raleigh. 2009. The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry. 48: 4707-4719.
    • (2009) Biochemistry. , vol.48 , pp. 4707-4719
    • Shan, B.1    Eliezer, D.2    Raleigh, D.P.3
  • 74
    • 60549110404 scopus 로고    scopus 로고
    • Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles
    • Weinkam, P., E. V. Pletneva, ..., P. G. Wolynes. 2009. Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles. Proc. Natl. Acad. Sci. USA. 106: 1796-1801.
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 1796-1801
    • Weinkam, P.1    Pletneva, E.V.2    Wolynes, P.G.3
  • 75
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254: 1598-1603.
    • (1991) Science. , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 76
    • 0037093654 scopus 로고    scopus 로고
    • Native and non-native interactions along protein folding and unfolding pathways
    • DOI 10.1002/prot.10089
    • Paci, E., M. Vendruscolo, and M. Karplus. 2002. Native and non-native interactions along protein folding and unfolding pathways. Proteins Struct. Funct. Genet. 47: 379-392. (Pubitemid 34438687)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.3 , pp. 379-392
    • Paci, E.1    Vendruscolo, M.2    Karplus, M.3
  • 78
    • 0035951080 scopus 로고    scopus 로고
    • Role of the chain termini for the folding transition state of the cold shock protein
    • DOI 10.1021/bi011378s
    • Perl, D., G. Holtermann, and F. X. Schmid. 2001. Role of the chain termini for the folding transition state of the cold shock protein. Biochemistry. 40: 15501-15511. (Pubitemid 34015177)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15501-15511
    • Perl, D.1    Holtermann, G.2    Schmid, F.X.3
  • 80
    • 45849127598 scopus 로고    scopus 로고
    • Barrierless evolution of structure during the submillisecond refolding reaction of a small protein
    • Sinha, K. K., and J. B. Udgaonkar. 2008. Barrierless evolution of structure during the submillisecond refolding reaction of a small protein. Proc. Natl. Acad. Sci. USA. 105: 7998-8003.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 7998-8003
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 82


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.