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Volumn 52, Issue 4, 2003, Pages 510-523

Simple two-state protein folding kinetics requires near-levinthal thermodynamic cooperativity

Author keywords

Calorimetric cooperativity; Chevron plot; Chevron rollover, non Arrhenius kinetics, G models; Contact order; Single domain proteins

Indexed keywords

PROTEIN; SINGLE DOMAIN PROTEIN; UNCLASSIFIED DRUG;

EID: 0042130544     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10506     Document Type: Article
Times cited : (69)

References (61)
  • 1
    • 0032559928 scopus 로고    scopus 로고
    • Matching speed and locality
    • Chan HS. Matching speed and locality. Nature 1998;392:761-763.
    • (1998) Nature , vol.392 , pp. 761-763
    • Chan, H.S.1
  • 2
    • 0034687123 scopus 로고    scopus 로고
    • Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
    • Plaxco KW, Simons KT, Ruczinski I, Baker D. Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics. Biochemistry 2000;39:11177-11183.
    • (2000) Biochemistry , vol.39 , pp. 11177-11183
    • Plaxco, K.W.1    Simons, K.T.2    Ruczinski, I.3    Baker, D.4
  • 3
    • 0002134029 scopus 로고    scopus 로고
    • Computational methods for protein folding: Scaling a hierarchy of complexities
    • Jiang T, Xu Y, Zhang MQ, editors. Cambridge, MA: The MIT Press
    • Chan HS, Kaya H, Shimizu S. Computational methods for protein folding: scaling a hierarchy of complexities. In: Jiang T, Xu Y, Zhang MQ, editors. Current Topics in Computational Molecular Biology. Cambridge, MA: The MIT Press; 2002. p 403-447.
    • (2002) Current Topics in Computational Molecular Biology , pp. 403-447
    • Chan, H.S.1    Kaya, H.2    Shimizu, S.3
  • 4
    • 0034284366 scopus 로고    scopus 로고
    • Modeling protein density of states: Additive hydrophobic effects are insufficient for calorimetric two-state cooperativity
    • Chan HS. Modeling protein density of states: additive hydrophobic effects are insufficient for calorimetric two-state cooperativity. Proteins 2000;40:543-571.
    • (2000) Proteins , vol.40 , pp. 543-571
    • Chan, H.S.1
  • 5
    • 0034284060 scopus 로고    scopus 로고
    • Polymer principles of protein calorimetric two-state cooperativity
    • Erratum: Proteins 2001;43:523
    • Kaya H, Chan HS. Polymer principles of protein calorimetric two-state cooperativity. Proteins 2000;40:637-661 [Erratum: Proteins 2001;43:523].
    • (2000) Proteins , vol.40 , pp. 637-661
    • Kaya, H.1    Chan, H.S.2
  • 6
    • 0034310589 scopus 로고    scopus 로고
    • Energetic components of cooperative protein folding
    • Kaya H, Chan HS. Energetic components of cooperative protein folding. Phys Rev Lett 2000;85:4823-4826.
    • (2000) Phys Rev Lett , vol.85 , pp. 4823-4826
    • Kaya, H.1    Chan, H.S.2
  • 7
    • 0036304480 scopus 로고    scopus 로고
    • Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: How applicable is the transition state picture to folding and unfolding?
    • Kaya H, Chan HS. Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: how applicable is the transition state picture to folding and unfolding? J Mol Biol 2002;315:899-909.
    • (2002) J Mol Biol , vol.315 , pp. 899-909
    • Kaya, H.1    Chan, H.S.2
  • 8
    • 0037459035 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling?
    • Kaya H, Chan HS. Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling? J Mol Biol 2003;326:911-931.
    • (2003) J Mol Biol , vol.326 , pp. 911-931
    • Kaya, H.1    Chan, H.S.2
  • 9
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go N. Theoretical studies of protein folding. Annu Rev Biophys Bioeng 1983;12:183-210.
    • (1983) Annu Rev Biophys Bioeng , vol.12 , pp. 183-210
    • Go, N.1
  • 10
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson JD, Wolynes PG, Spin glasses and the statistical mechanics of protein folding. Proc Natl Acad Sci USA 1987;84:7524-7528.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 11
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. 1. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi H, Ueda Y, Go N. Studies on protein folding, unfolding and fluctuations by computer simulation. 1. The effect of specific amino acid sequence represented by specific inter-unit interactions. Int J Pept Protein Res 1975;7:445-459.
    • (1975) Int J Pept Protein Res , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 12
    • 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, Nymeyer H, Onuchic JN. 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 2000;298:937-953.
    • (2000) J Mol Biol , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 13
    • 0035818481 scopus 로고    scopus 로고
    • Constructing, verifying, and dissecting the folding transition state of chymotrypsin inhibitor 2 with all-atom simulations
    • Li L, Shakhnovich EI. Constructing, verifying, and dissecting the folding transition state of chymotrypsin inhibitor 2 with all-atom simulations. Proc Natl Acad Sci USA 2001;98:13014-13018.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13014-13018
    • Li, L.1    Shakhnovich, E.I.2
  • 14
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory ofprotein folding rates. II. Local reaction coordinates and chain dynamics
    • Portman JJ, Takada S, Wolynes PG. Microscopic theory ofprotein folding rates. II. Local reaction coordinates and chain dynamics. J Chem Phys 2001;114:5082-5096.
    • (2001) J Chem Phys , vol.114 , pp. 5082-5096
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 15
    • 0036385839 scopus 로고    scopus 로고
    • Elastic properties of proteins: Insight on the folding process and evolutionary selection of native structures
    • Micheletti C, Lattanzi G, Maritan A. Elastic properties of proteins: insight on the folding process and evolutionary selection of native structures. J Mol Biol 2002;321:909-921.
    • (2002) J Mol Biol , vol.321 , pp. 909-921
    • Micheletti, C.1    Lattanzi, G.2    Maritan, A.3
  • 16
    • 0037113227 scopus 로고    scopus 로고
    • The role of sidechain packing and native contact interactions in folding: Discontinuous molecular dynamics folding simulations of an all-atom Gō model of fragment B of Staphylococcal protein A
    • Linhananta A, Zhou Y. The role of sidechain packing and native contact interactions in folding: discontinuous molecular dynamics folding simulations of an all-atom Gō model of fragment B of Staphylococcal protein A. J Chem Phys 2002;117:8983-8995.
    • (2002) J Chem Phys , vol.117 , pp. 8983-8995
    • Linhananta, A.1    Zhou, Y.2
  • 17
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco KW, Simons KT, Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 1998;227:985-994.
    • (1998) J Mol Biol , vol.227 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 18
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews CR. Effect of point mutations on the folding of globular proteins. Methods Enzymol 1987; 154:498-511.
    • (1987) Methods Enzymol , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 19
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung MS, Garcia AE, Onuchic JN. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc Natl Acad Sci USA 2002;99:685-690.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 685-690
    • Cheung, M.S.1    Garcia, A.E.2    Onuchic, J.N.3
  • 20
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 21
    • 0029809182 scopus 로고    scopus 로고
    • On the origin of the cooperativity of protein folding: Implications from model simulations
    • Kolinski A, Galazka W, Skolnick J. On the origin of the cooperativity of protein folding: implications from model simulations. Proteins 1996;26:271-287.
    • (1996) Proteins , vol.26 , pp. 271-287
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 22
    • 0007463680 scopus 로고    scopus 로고
    • Statistical mechanics of a correlated energy landscape model for protein folding funnels
    • Plotkin SS, Wang J, Wolynes PG. Statistical mechanics of a correlated energy landscape model for protein folding funnels, J Chem Phys 1997; 106:2932-2948.
    • (1997) J Chem Phys , vol.106 , pp. 2932-2948
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 23
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler T, Schmid FX. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry 1996;35:16833-16842.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 24
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley ML, Baker D. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc Natl Acad Sci USA 1997;94:10636-10640.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 25
    • 36448999595 scopus 로고
    • Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice model simulations
    • Abkevich VI, Gutin AM, Shakhnovich EI. Free energy landscape for protein folding kinetics: intermediates, traps, and multiple pathways in theory and lattice model simulations. J Chem Phys 1994;101:6052-6062.
    • (1994) J Chem Phys , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 26
    • 0002353848 scopus 로고    scopus 로고
    • Modelling protein folding by Monte Carlo dynamics: Chevron plots, chevron rollover, and non-Arrhenius kinetics
    • Grassberger P, Barkema GT, Nadler W, editors. Singapore: World Scientific
    • Chan HS. Modelling protein folding by Monte Carlo dynamics: chevron plots, chevron rollover, and non-Arrhenius kinetics, In: Grassberger P, Barkema GT, Nadler W, editors. Monte Carlo Approach to Biopolymers and Protein Folding. Singapore: World Scientific; 1998. p 29-44.
    • (1998) Monte Carlo Approach to Biopolymers and Protein Folding , pp. 29-44
    • Chan, H.S.1
  • 27
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan HS, Dill KA. Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins 1998;30:2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 28
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • Northey JGB, Di Nardo AA, Davidson AR. Hydrophobic core packing in the SH3 domain folding transition state. Nat Struct Biol 2002;9:126-130.
    • (2002) Nat Struct Biol , vol.9 , pp. 126-130
    • Northey, J.G.B.1    Di Nardo, A.A.2    Davidson, A.R.3
  • 29
    • 0036266942 scopus 로고    scopus 로고
    • Conformational strain in the hydrophobic core and its implications for protein folding and design
    • Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L. Conformational strain in the hydrophobic core and its implications for protein folding and design. Nat Struct Biol 2002;9:485-493.
    • (2002) Nat Struct Biol , vol.9 , pp. 485-493
    • Ventura, S.1    Vega, M.C.2    Lacroix, E.3    Angrand, I.4    Spagnolo, L.5    Serrano, L.6
  • 30
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Gō-like model
    • Koga N, Takada S. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Gō-like model. J Mol Biol 2001;313:171-180.
    • (2001) J Mol Biol , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 31
    • 0037423710 scopus 로고    scopus 로고
    • Cooperativity, smooth energy landscapes and the origins of topology-dependent protein folding rates
    • Jewett AI, Pande VS, Plaxco KW. Cooperativity, smooth energy landscapes and the origins of topology-dependent protein folding rates. J Mol Biol 2003;326:247-253.
    • (2003) J Mol Biol , vol.326 , pp. 247-253
    • Jewett, A.I.1    Pande, V.S.2    Plaxco, K.W.3
  • 32
    • 0036678120 scopus 로고    scopus 로고
    • Experimental evaluation of topological parameters determining protein-folding rates
    • Miller EJ, Fischer KF, Marqusee S. Experimental evaluation of topological parameters determining protein-folding rates. Proc Natl Acad Sci USA 2002;99:10359-10363.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10359-10363
    • Miller, E.J.1    Fischer, K.F.2    Marqusee, S.3
  • 33
    • 0042631521 scopus 로고    scopus 로고
    • Contact order dependent protein folding rates: Kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences
    • Kaya H, Chan HS. Contact order dependent protein folding rates: kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences. Proteins 2003;52:524-533.
    • (2003) Proteins , vol.52 , pp. 524-533
    • Kaya, H.1    Chan, H.S.2
  • 34
    • 0042598668 scopus 로고    scopus 로고
    • Cooperativity principles in protein folding
    • Forthcoming
    • Chan HS, Shimizu S, Kaya H. Cooperativity principles in protein folding. Methods Enzymol 2003. Forthcoming,
    • (2003) Methods Enzymol
    • Chan, H.S.1    Shimizu, S.2    Kaya, H.3
  • 35
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • Segawa S, Sugihara M. Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state. Biopolymers 1984;23:2473-2488.
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.1    Sugihara, M.2
  • 36
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen B-L, Baase WA, Schellman JA. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 1989;28:691-699.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.-L.1    Baase, W.A.2    Schellman, J.A.3
  • 37
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson SE, Fersht AR. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 1991;30:10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 38
    • 0032545150 scopus 로고    scopus 로고
    • Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
    • Kuhlman B, Luisi DL, Evans PA, Raleigh DP. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. J Mol Biol 1998;284:1661-1670.
    • (1998) J Mol Biol , vol.284 , pp. 1661-1670
    • Kuhlman, B.1    Luisi, D.L.2    Evans, P.A.3    Raleigh, D.P.4
  • 40
    • 36549099780 scopus 로고
    • The structure of liquid water at an extended hydrophobic surface
    • Lee CY, McCammon JA, Rossky PJ. The structure of liquid water at an extended hydrophobic surface. J Chem Phys 1984;80:4448-4455.
    • (1984) J Chem Phys , vol.80 , pp. 4448-4455
    • Lee, C.Y.1    McCammon, J.A.2    Rossky, P.J.3
  • 41
    • 0011960339 scopus 로고    scopus 로고
    • Hydrophobicity at small and large length scales
    • Lum K, Chandler D, Weeks JD. Hydrophobicity at small and large length scales. J Phys Chem B 1999;103:4570-4577.
    • (1999) J Phys Chem B , vol.103 , pp. 4570-4577
    • Lum, K.1    Chandler, D.2    Weeks, J.D.3
  • 42
    • 0036891682 scopus 로고    scopus 로고
    • Origins of protein denatured states compactness and hydrophobic clustering in aqueous urea: Inferences from nonpolar potentials of mean force
    • Shimizu S, Chan HS. Origins of protein denatured states compactness and hydrophobic clustering in aqueous urea: inferences from nonpolar potentials of mean force. Proteins 2002;49:560-566.
    • (2002) Proteins , vol.49 , pp. 560-566
    • Shimizu, S.1    Chan, H.S.2
  • 43
    • 0028387381 scopus 로고
    • Folding intermediates in protein folding
    • Baldwin RL. Folding intermediates in protein folding. BioEssays 1994;16:207-210.
    • (1994) BioEssays , vol.16 , pp. 207-210
    • Baldwin, R.L.1
  • 44
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 1995;21:167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 45
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol 1997;4:10-19.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 46
    • 0042093787 scopus 로고    scopus 로고
    • Origins of chevron rollovers in non-two-state protein folding kinetics
    • Kaya H, Chan HS. Origins of chevron rollovers in non-two-state protein folding kinetics. Phys Rev Lett 2003;90:258104.
    • (2003) Phys Rev Lett , vol.90 , pp. 258104
    • Kaya, H.1    Chan, H.S.2
  • 47
    • 0036643497 scopus 로고    scopus 로고
    • Anti-cooperativity and cooperativity in hydrophobic interactions: Three-body free energy landscapes and comparison with implicit-solvent potential functions for proteins
    • Erratum: Proteins 2002;49:2941
    • Shimizu S, Chan HS. Anti-cooperativity and cooperativity in hydrophobic interactions: three-body free energy landscapes and comparison with implicit-solvent potential functions for proteins. Proteins 2002;48:15-30 [Erratum: Proteins 2002;49:2941.
    • (2002) Proteins , vol.48 , pp. 15-30
    • Shimizu, S.1    Chan, H.S.2
  • 48
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
    • Makarov DE, Plaxco KW. The topomer search model: a simple, quantitative theory of two-state protein folding kinetics. Protein Sci 2003;12:17-26.
    • (2003) Protein Sci , vol.12 , pp. 17-26
    • Makarov, D.E.1    Plaxco, K.W.2
  • 49
    • 0036469703 scopus 로고    scopus 로고
    • Lattice models ofprotein folding permitting disordered native states
    • Crippen GM, Chhajer M. Lattice models ofprotein folding permitting disordered native states. J Chem Phys 2002;116:2261-2268.
    • (2002) J Chem Phys , vol.116 , pp. 2261-2268
    • Crippen, G.M.1    Chhajer, M.2
  • 50
    • 0043094427 scopus 로고    scopus 로고
    • Folding of lattice protein chains with modified Gō potential
    • Fan K, Wang J, Wang W. Folding of lattice protein chains with modified Gō potential. Eur Phys J B 2002;30:381-391.
    • (2002) Eur Phys J B , vol.30 , pp. 381-391
    • Fan, K.1    Wang, J.2    Wang, W.3
  • 51
    • 0037459022 scopus 로고    scopus 로고
    • Interplay among tertiary contacts, secondary structure formation and side-chain packing in the protein folding mechanism: All-atom representation study of protein L
    • Clementi C, Garcia AE, Onuchic JN. Interplay among tertiary contacts, secondary structure formation and side-chain packing in the protein folding mechanism: all-atom representation study of protein L. J Mol Biol 2003;326:933-954.
    • (2003) J Mol Biol , vol.326 , pp. 933-954
    • Clementi, C.1    Garcia, A.E.2    Onuchic, J.N.3
  • 52
    • 0037343134 scopus 로고    scopus 로고
    • A minimal physically realistic protein-like lattice model: Designing an energy landscape that ensures all-or-none folding to a unique native state
    • Pokarowski P, Kolinski A, Skolnick J. A minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native state. Biophys J 2003;84:1518-1526.
    • (2003) Biophys J , vol.84 , pp. 1518-1526
    • Pokarowski, P.1    Kolinski, A.2    Skolnick, J.3
  • 53
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstrφm-Lang
    • Englander SW, Mayne L, Bai Y, Sosnick TR. Hydrogen exchange: the modern legacy of Linderstrφm-Lang. Protein Sci 1997;6:1101-1109.
    • (1997) Protein Sci , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 54
    • 0001504441 scopus 로고    scopus 로고
    • Cooperativity in protein folding: From lattice models with sidechains to real proteins
    • Klimov DK, Thirumalai D. Cooperativity in protein folding: from lattice models with sidechains to real proteins. Fold Des 1998;3:127-139.
    • (1998) Fold Des , vol.3 , pp. 127-139
    • Klimov, D.K.1    Thirumalai, D.2
  • 55
    • 0037079586 scopus 로고    scopus 로고
    • Is there a unique melting temperature for two-state proteins?
    • Klimov DK, Thirumalai D. Is there a unique melting temperature for two-state proteins? J Comput Chem 2002;23:161-165.
    • (2002) J Comput Chem , vol.23 , pp. 161-165
    • Klimov, D.K.1    Thirumalai, D.2
  • 56
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • Zwanzig R. Simple model of protein folding kinetics. Proc Natl Acad Sci USA 1995;92:9801-9804.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 57
    • 0031557390 scopus 로고    scopus 로고
    • Factors affecting the ability of energy functions to discriminate correct from incorrect folds
    • Park BH, Huang ES, Levitt M. Factors affecting the ability of energy functions to discriminate correct from incorrect folds. J Mol Biol 1997;266:831-846.
    • (1997) J Mol Biol , vol.266 , pp. 831-846
    • Park, B.H.1    Huang, E.S.2    Levitt, M.3
  • 58
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack RL. Rotamer libraries in the 21st century. Curr Opin Struct Biol 2002;12:431-440.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 431-440
    • Dunbrack, R.L.1
  • 60
    • 0037402639 scopus 로고    scopus 로고
    • Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics
    • Galzitskaya OV, Garbuzynskiy SO, Ivankov DN, Finkelstein AV. Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics. Proteins 2003;51:162-166.
    • (2003) Proteins , vol.51 , pp. 162-166
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Ivankov, D.N.3    Finkelstein, A.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.