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Volumn 1, Issue 1, 2004, Pages 23-56

Physics of protein folding

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EID: 3042638519     PISSN: 15710645     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plrev.2004.03.001     Document Type: Review
Times cited : (107)

References (174)
  • 2
    • 36949066642 scopus 로고
    • Structure of hemoglobin: The three-dimensional Fourier synthesis at 5.5 Å resolution, obtained by X-ray analysis
    • Perutz MF, Rossmann MG, Cullis AF, Muirhead G, Will G, North T. Structure of hemoglobin: the three-dimensional Fourier synthesis at 5.5 Å resolution, obtained by X-ray analysis. Nature 1960; 185:416-22.
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, G.4    Will, G.5    North, T.6
  • 3
    • 0003919736 scopus 로고
    • NMR of Proteins and Nucleic Acids
    • New York: Wiley
    • Wüthrich K. NMR of Proteins and Nucleic Acids. New York: Wiley; 1986.
    • (1986)
    • Wüthrich, K.1
  • 4
    • 67349189383 scopus 로고
    • The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
    • Anfinsen CB, Haber E, Sela M, White FH. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl. Acad. Sci. USA 1961;47:1309-14.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1309-1314
    • Anfinsen, C.B.1    Haber, E.2    Sela, M.3    White, F.H.4
  • 5
    • 0014675276 scopus 로고
    • The total synthesis of an enzyme with ribonuclease A activity
    • Gutte B, Merrifield RB. The total synthesis of an enzyme with ribonuclease A activity. J. Am. Chem. Soc. 1969;91:501-2.
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 501-502
    • Gutte, B.1    Merrifield, R.B.2
  • 6
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 1974;86:665-84.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 8
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991;24:946-50.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 10
    • 3042601793 scopus 로고    scopus 로고
    • Proteins: Thermodynamic, structural and kinetic aspects
    • Barrat J-L, Feigelman M, Kurchan J, Dalibard J, editors. UFJ NATO ASI. Les Houches, Session 77, 2002. Les Ulis-Paris-Cambridge: EDP Sciences. Berlin-Heidelberg-New York-Hong Kong-London -Milan-Paris-Tokyo: Springer-Verlag
    • Finkelstein AV. Proteins: Thermodynamic, structural and kinetic aspects. In: Barrat J-L, Feigelman M, Kurchan J, Dalibard J, editors. UFJ NATO ASI. Les Houches, Session 77, 2002. Slow Relaxations and Nonequilibrium Dynamics in Condenced Matter. Les Ulis-Paris-Cambridge: EDP Sciences. Berlin-Heidelberg-New York-Hong Kong-London -Milan-Paris-Tokyo: Springer-Verlag; 2003, p. 649-704.
    • (2003) Slow Relaxations and Nonequilibrium Dynamics in Condenced Matter , pp. 649-704
    • Finkelstein, A.V.1
  • 11
    • 0004155427 scopus 로고
    • Biochemistry
    • Four ed. New York: Freeman
    • Stryer L. Biochemistry. Four ed. New York: Freeman; 1995.
    • (1995)
    • Stryer, L.1
  • 12
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • Kolb VA, Makeev EV, Spirin AS. Folding of firefly luciferase during translation in a cell-free system. EMBO J. 1994;13:3631-7.
    • (1994) EMBO J. , vol.13 , pp. 3631-3637
    • Kolb, V.A.1    Makeev, E.V.2    Spirin, A.S.3
  • 13
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis RJ, Hartl FU. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 1999;9:102-10.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 15
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding?. J. Chim. Phys. PCB 1968;65:44-5.
    • (1968) J. Chim. Phys. PCB , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 16
    • 0013971370 scopus 로고
    • The three-dimensional structure of an enzyme molecule
    • Phillips DC. The three-dimensional structure of an enzyme molecule. Sci. Am. 1966;215:78-90.
    • (1966) Sci. Am. , vol.215 , pp. 78-90
    • Phillips, D.C.1
  • 17
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 1983;165:407-13.
    • (1983) J. Mol. Biol. , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 18
    • 0021659554 scopus 로고
    • Folding pathway of a circular form of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE. Folding pathway of a circular form of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 1984;179:527-45.
    • (1984) J. Mol. Biol. , vol.179 , pp. 527-545
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 19
    • 0015920746 scopus 로고
    • Stages in the mechanism of self-organization of protein molecules
    • Ptitsyn OB. Stages in the mechanism of self-organization of protein molecules. Dokl. AN SSSR 1973;210:1213-5.
    • (1973) Dokl. AN SSSR , vol.210 , pp. 1213-1215
    • Ptitsyn, O.B.1
  • 20
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. Molten globule and protein folding. Adv. Protein Chem. 1995;47:83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 21
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright PE, Dyson HJ, Lerner RA. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry 1988;27:7167-75.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3
  • 22
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29:7133-55.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 23
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin RL, Rose GD. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem. Sci. 1999;24:26-33.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 24
    • 0034669844 scopus 로고    scopus 로고
    • Mechanism of protein folding
    • Nölting B, Andret K. Mechanism of protein folding. Proteins 2000;41:288-98.
    • (2000) Proteins , vol.41 , pp. 288-298
    • Nölting, B.1    Andret, K.2
  • 26
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson HJ, Rance M, Houghten RA, Wright PE, Lerner RA. Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J. Mol. Biol. 1988;201:201-17.
    • (1988) J. Mol. Biol. , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 28
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable beta-hairpin in aqueous solution
    • Blanco FJ, Rivas G, Serrano L. A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat. Struc. Biol. 1994;1:584-90.
    • (1994) Nat. Struc. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 32
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA 1997;94:3709-13.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 33
    • 0016803266 scopus 로고
    • On the rate determining step for helix propagation in the helix-coil transition of polypeptides in solution
    • Zana R. On the rate determining step for helix propagation in the helix-coil transition of polypeptides in solution. Biopolymers 1975;14:2425-8.
    • (1975) Biopolymers , vol.14 , pp. 2425-2428
    • Zana, R.1
  • 34
    • 78651171134 scopus 로고
    • On the kinetics of helix-coil transition of polypeptides in solution
    • Schwarz G. On the kinetics of helix-coil transition of polypeptides in solution. J. Mol. Biol. 1965;11:64-77.
    • (1965) J. Mol. Biol. , vol.11 , pp. 64-77
    • Schwarz, G.1
  • 35
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm BH, Bragg JR. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 1959;31:526-35.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.R.2
  • 36
    • 0015272079 scopus 로고
    • Thermodynamic parameters of helix-coil transition in polypeptide chains
    • Ptitsyn OB. Thermodynamic parameters of helix-coil transition in polypeptide chains. Pure Appl. Chem. 1972;31:227-44.
    • (1972) Pure Appl. Chem. , vol.31 , pp. 227-244
    • Ptitsyn, O.B.1
  • 38
    • 0036250489 scopus 로고    scopus 로고
    • α-helix and β-hairpin folding from experiment, analytical theory and molecular dynamics simulations
    • Galzitskaya OV, Higo J, Finkelstein AV. α-helix and β-hairpin folding from experiment, analytical theory and molecular dynamics simulations. Curr. Protein Pept. Sci. 2002;3:191-200.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 191-200
    • Galzitskaya, O.V.1    Higo, J.2    Finkelstein, A.V.3
  • 39
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Munoz V, Thompson PA, Hofrichter J, Eaton WA. Folding dynamics and mechanism of beta-hairpin formation. Nature 1997;390:196-9.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 41
    • 0016134860 scopus 로고
    • Beta poly(L-lysine): A model system for biological self-assembly
    • Hartman R, Schwaner RC, Hermans Jr. J. Beta poly(L-lysine): A model system for biological self-assembly. J. Mol. Biol. 1974;90:415-29.
    • (1974) J. Mol. Biol. , vol.90 , pp. 415-429
    • Hartman, R.1    Schwaner, R.C.2    Hermans Jr., J.3
  • 42
    • 0009019420 scopus 로고
    • Correlation between rate or chain folding and stability of the β-structure of a polypeptide
    • Fukada K, Maeda H. Correlation between rate or chain folding and stability of the β-structure of a polypeptide. J. Phys. Chem. 1990;94:3843-7.
    • (1990) J. Phys. Chem. , vol.94 , pp. 3843-3847
    • Fukada, K.1    Maeda, H.2
  • 43
    • 0009015527 scopus 로고
    • Kinetics of formation of anti parallel β-structure
    • Finkelstein AV. Kinetics of formation of anti parallel β-structure. Bioorgan. Khim. (Russia) 1978;4:340-4.
    • (1978) Bioorgan. Khim. (Russia) , vol.4 , pp. 340-344
    • Finkelstein, A.V.1
  • 44
    • 0026019655 scopus 로고
    • Rate of β-structure formation in polypeptides
    • Finkelstein AV. Rate of β-structure formation in polypeptides. Proteins 1991;9:23-7.
    • (1991) Proteins , vol.9 , pp. 23-27
    • Finkelstein, A.V.1
  • 45
    • 0017188253 scopus 로고
    • Intramolecular conformational transitions "Random coil-helix-folded structure" in polypeptides
    • Adonts VG, Birshtein TM, Elyashevich AM, Skvortsov AM. Intramolecular conformational transitions "random coil-helix-folded structure" in polypeptides. Biopolymers 1976;15:1037-59.
    • (1976) Biopolymers , vol.15 , pp. 1037-1059
    • Adonts, V.G.1    Birshtein, T.M.2    Elyashevich, A.M.3    Skvortsov, A.M.4
  • 47
    • 0004049753 scopus 로고
    • Melting and Crystal Structure
    • Oxford: Clarendon
    • Ubbelohde AR. Melting and Crystal Structure. Oxford: Clarendon; 1965.
    • (1965)
    • Ubbelohde, A.R.1
  • 48
    • 0017823384 scopus 로고
    • Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism
    • Kuwajima K, Sugai S. Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism. Biophys. Chem. 1978;8:247-54.
    • (1978) Biophys. Chem. , vol.8 , pp. 247-254
    • Kuwajima, K.1    Sugai, S.2
  • 51
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL. Stability of proteins: small globular proteins. Adv. Prot. Chem. 1979;33:167-241.
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 52
    • 0022445353 scopus 로고
    • Physical nature of the phase transition in globular proteins: Calorimetric study of human alpha-lactalbumin
    • Pfeil W, Bychkova VE, Ptitsyn OB. Physical nature of the phase transition in globular proteins: Calorimetric study of human alpha-lactalbumin. FEBS Lett. 1986;198:287-91.
    • (1986) FEBS Lett. , vol.198 , pp. 287-291
    • Pfeil, W.1    Bychkova, V.E.2    Ptitsyn, O.B.3
  • 53
    • 0024742246 scopus 로고
    • Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition
    • Shakhnovich EI, Finkelstein AV. Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers 1989;28:1667-80.
    • (1989) Biopolymers , vol.28 , pp. 1667-1680
    • Shakhnovich, E.I.1    Finkelstein, A.V.2
  • 54
    • 0024745242 scopus 로고
    • Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution
    • Finkelstein AV, Shakhnovich EI. Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers 1989;28:1681-94.
    • (1989) Biopolymers , vol.28 , pp. 1681-1694
    • Finkelstein, A.V.1    Shakhnovich, E.I.2
  • 55
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Prot. Chem. 1968;23:121-282.
    • (1968) Adv. Prot. Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 56
    • 0003932766 scopus 로고
    • Proteins
    • Second ed. New York: Freeman
    • Creighton TE. Proteins. Second ed. New York: Freeman; 1991.
    • (1991)
    • Creighton, T.E.1
  • 57
    • 0028466243 scopus 로고
    • Protein folding. Solid evidence for molten globules
    • Dobson CM. Protein folding. Solid evidence for molten globules. Curr. Biol. 1994;4:636-40.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 58
    • 0030330918 scopus 로고    scopus 로고
    • Insights into protein folding from NMR
    • Dyson HJ, Wright PE. Insights into protein folding from NMR. Ann. Rev. Phys. Chem. 1996;47:369-95.
    • (1996) Ann. Rev. Phys. Chem. , vol.47 , pp. 369-395
    • Dyson, H.J.1    Wright, P.E.2
  • 60
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson SE. How do small single-domain proteins fold?. Fold. Des. 1998;3:R81-91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 62
    • 0023642620 scopus 로고
    • An early intermediate of refolding alpha-lactalbumin forms within 20 ms
    • Gilmanshin RI, Ptitsyn OB. An early intermediate of refolding alpha-lactalbumin forms within 20 ms. FEBS Lett. 1987;223:327-9.
    • (1987) FEBS Lett. , vol.223 , pp. 327-329
    • Gilmanshin, R.I.1    Ptitsyn, O.B.2
  • 63
    • 0023669402 scopus 로고
    • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
    • Kuwajima K, Yamaya H, Miwa S, Sugai S. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 1987;227:115-8.
    • (1987) FEBS Lett. , vol.227 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4
  • 64
    • 0028176911 scopus 로고
    • "Partly folded" state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature
    • Uversky VN, Ptitsyn OB. "Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. Biochemistry 1994;33:2782-91.
    • (1994) Biochemistry , vol.33 , pp. 2782-2791
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 65
    • 0029924194 scopus 로고    scopus 로고
    • Further evidence on the equilibrium "pre-molten globule state": Four-state GdmCl-induced unfolding of carbonic anhydrase B at low temperature
    • Uversky VN, Ptitsyn OB. Further evidence on the equilibrium "pre-molten globule state": four-state GdmCl-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol. 1996; 255:215-28.
    • (1996) J. Mol. Biol. , vol.255 , pp. 215-228
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 66
    • 0030817794 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics and structure of the I form of apomyoglobin
    • Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobin. Biochemistry 1997;36:15006-12.
    • (1997) Biochemistry , vol.36 , pp. 15006-15012
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 67
    • 0032067753 scopus 로고    scopus 로고
    • The core of apomyoglobin E-form folds at the diffusion limit
    • Gilmanshin R, Callender RH, Dyer RB. The core of apomyoglobin E-form folds at the diffusion limit. Nat. Struct. Biol. 1998;5:363-5.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 363-365
    • Gilmanshin, R.1    Callender, R.H.2    Dyer, R.B.3
  • 68
    • 0007291003 scopus 로고
    • Jaenicke R, editor. Amsterdam-New York: Elsevier
    • Baldwin RL, Creighton TE. In: Jaenicke R, editor. Protein Folding. Amsterdam-New York: Elsevier; 1980, p. 217-60.
    • (1980) Protein Folding , pp. 217-260
    • Baldwin, R.L.1    Creighton, T.E.2
  • 69
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • Segawa S-I, Sugihara M. Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state. Biopolymers 1984;23:2473-88.
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.-I.1    Sugihara, M.2
  • 70
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov PL. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 1982;35:1-104
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 71
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht AR. Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 1995;5:79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 72
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson CM, Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 1999;9:92-101.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 74
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht AR. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 1997;7:3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 77
    • 0030623529 scopus 로고    scopus 로고
    • Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
    • Finkelstein AV, Badretdinov AYa. Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Fold. Des. 1997;2:115-21.
    • (1997) Fold. Des. , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Ya.2
  • 78
    • 0025148817 scopus 로고
    • A simple statistical field theory of heteropolymer collapse with application to protein folding
    • Bryngelson JD, Wolynes PG. A simple statistical field theory of heteropolymer collapse with application to protein folding. Biopolymers 1990;30:177-88.
    • (1990) Biopolymers , vol.30 , pp. 177-188
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 81
    • 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;84:7524-8.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 82
    • 84956127383 scopus 로고
    • Mean-field model for protein folding
    • Garel T, Orland H. Mean-field model for protein folding. Europhys. Lett. 1988;6:307-10.
    • (1988) Europhys. Lett. , vol.6 , pp. 307-310
    • Garel, T.1    Orland, H.2
  • 83
    • 0024357911 scopus 로고
    • Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach
    • Shakhnovich EE, Gutin AM. Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach. Biophys. Chem. 1989;34:187-99.
    • (1989) Biophys. Chem. , vol.34 , pp. 187-199
    • Shakhnovich, E.E.1    Gutin, A.M.2
  • 84
    • 4243861085 scopus 로고
    • Random-Energy model: An exactly solvable model of disordered systems
    • Derrida B. Random-Energy model: an exactly solvable model of disordered systems. Phys. Rev. B 1981;24:2613-26.
    • (1981) Phys. Rev. B , vol.24 , pp. 2613-2626
    • Derrida, B.1
  • 85
    • 0043230411 scopus 로고
    • Spin glasses: Experimental facts, theoretical concepts, and open questions
    • Binder K, Young AP. Spin glasses: experimental facts, theoretical concepts, and open questions. Rev. Mod. Phys. 1986;58:801-976.
    • (1986) Rev. Mod. Phys. , vol.58 , pp. 801-976
    • Binder, K.1    Young, A.P.2
  • 86
    • 0028270634 scopus 로고
    • Kinetics of protein folding - A lattice model study of the requirements for folding to the native state
    • Šali A, Shakhnovich EI, Karplus M. Kinetics of protein folding - a lattice model study of the requirements for folding to the native state. J. Mol. Biol. 1994;235:1614-36.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Šali, A.1    Shakhnovich, E.I.2    Karplus, M.3
  • 87
    • 0025146274 scopus 로고
    • Implications of thermodynamics of protein folding for evolution of primary sequences
    • Shakhnovich EI, Gutin AM. Implications of thermodynamics of protein folding for evolution of primary sequences. Nature 1990;346:773-5.
    • (1990) Nature , vol.346 , pp. 773-775
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 89
    • 0002394256 scopus 로고    scopus 로고
    • Influence of chain knotting on the rate of folding
    • Finkelstein AV, Badretdinov AYa. Influence of chain knotting on the rate of folding. Fold. Des. 1998;3:67-8.
    • (1998) Fold. Des. , vol.3 , pp. 67-68
    • Finkelstein, A.V.1    Badretdinov, A.Ya.2
  • 90
    • 0004101795 scopus 로고
    • Physical Kinetics
    • London: Pergamon
    • Lifshiz EM, Pitaevskii LP. Physical Kinetics. London: Pergamon; 1981.
    • (1981)
    • Lifshiz, E.M.1    Pitaevskii, L.P.2
  • 91
    • 0016812958 scopus 로고
    • Theory of reversible denaturation of globular proteins
    • Go N. Theory of reversible denaturation of globular proteins. Int. J. Pept. Prot. Res. 1975;7:313-23.
    • (1975) Int. J. Pept. Prot. Res. , vol.7 , pp. 313-323
    • Go, N.1
  • 92
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go N. Theoretical studies of protein folding. Ann. Rev. Biophys. Bioeng. 1983;12:183-210.
    • (1983) Ann. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 93
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • Thirumalai D. From minimal models to real proteins: time scales for protein folding kinetics. J. Phys. 1995;5:1457-67.
    • (1995) J. Phys. , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 96
    • 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;277:985-94.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 97
    • 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;101:6052-62.
    • (1994) J. Chem. Phys. , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 98
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin AM, Abkevich VI, Shakhnovich EI. Is burst hydrophobic collapse necessary for protein folding?. Biochemistry 1995;34:3066-76.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 99
    • 0028024928 scopus 로고
    • Specific nucleus as a transition state for protein folding: An evidence from lattice model
    • Abkevich VI, Gutin AM, Shakhnovich EI. Specific nucleus as a transition state for protein folding: an evidence from lattice model. Biochemistry 1994;33:10026-36.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 100
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger proteins within the capillarity approximation
    • Wolynes PG. Folding funnels and energy landscapes of larger proteins within the capillarity approximation. Proc. Natl. Acad. Sci. USA 1997;94:6170-5.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1
  • 101
    • 0034799915 scopus 로고    scopus 로고
    • Cunning simplicity of protein folding landscapes
    • Bogatyreva NS, Finkelstein AV. Cunning simplicity of protein folding landscapes. Protein Eng. 2001;14:521-3.
    • (2001) Protein Eng. , vol.14 , pp. 521-523
    • Bogatyreva, N.S.1    Finkelstein, A.V.2
  • 102
    • 0036674529 scopus 로고    scopus 로고
    • Loop fold structure of proteins: Resolution of Levinthas paradox
    • Berezovsky IN, Trifonov EN. Loop fold structure of proteins: resolution of Levinthas paradox. J. Biomol. Struct. Dyn. 2002;20:5-6.
    • (2002) J. Biomol. Struct. Dyn. , vol.20 , pp. 5-6
    • Berezovsky, I.N.1    Trifonov, E.N.2
  • 103
    • 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
  • 104
    • 0034021174 scopus 로고    scopus 로고
    • Entropic barriers, transition states, funnels, and exponential protein folding kinetics: A simple model
    • Bicout DJ, Szabo A. Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model. Protein Sci. 2000;9:452-65.
    • (2000) Protein Sci. , vol.9 , pp. 452-465
    • Bicout, D.J.1    Szabo, A.2
  • 105
    • 0028937232 scopus 로고
    • Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms
    • Sancho E, Declerck PJ, Price NC, Kelly SM, Booth NA. Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms. J. Mol. Biol. 1995;34:1064-9.
    • (1995) J. Mol. Biol. , vol.34 , pp. 1064-1069
    • Sancho, E.1    Declerck, P.J.2    Price, N.C.3    Kelly, S.M.4    Booth, N.A.5
  • 106
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model
    • Thompson PA, Eaton WA, Hofrichter J. Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. J. Mol. Biol. 1997;36:9200-10.
    • (1997) J. Mol. Biol. , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 108
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A, Kellis JT Jr., Serrano L, Fersht AR. Mapping the transition state and pathway of protein folding by protein engineering. Nature 1989;340:122-6.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 109
    • 0003558028 scopus 로고
    • Rates and Equilibria of Organic Chemistry
    • New York: Dover
    • Leffler JE, Grunwald E. Rates and Equilibria of Organic Chemistry. New York: Dover; 1963.
    • (1963)
    • Leffler, J.E.1    Grunwald, E.2
  • 110
    • 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;154:127-32.
    • (1987) Methods Enzymol. , vol.154 , pp. 127-132
    • Matthews, C.R.1
  • 112
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht AR, Matouschek A, Serrano L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 1992;224:771-82.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 113
    • 0033580679 scopus 로고    scopus 로고
    • Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots
    • Otzen DE, Kristensen O, Proctor M, Oliveberg M. Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots. Biochemistry 1999;38:6499-511.
    • (1999) Biochemistry , vol.38 , pp. 6499-6511
    • Otzen, D.E.1    Kristensen, O.2    Proctor, M.3    Oliveberg, M.4
  • 114
    • 0034112774 scopus 로고    scopus 로고
    • Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus
    • Li L, Mirny LA, Shakhnovich EI. Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus. Nat. Struc. Biol. 2000;7:336-42.
    • (2000) Nat. Struc. Biol. , vol.7 , pp. 336-342
    • Li, L.1    Mirny, L.A.2    Shakhnovich, E.I.3
  • 115
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki LS, Otzen DT, Fersht AR. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 1995;254:260-88.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.T.2    Fersht, A.R.3
  • 116
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR. Structure of the transition state for folding of a protein derived from experiment and simulation. J. Mol. Biol. 1996;257:430-40.
    • (1996) J. Mol. Biol. , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 117
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich E, Abkevich V, Ptitsyn O. Conserved residues and the mechanism of protein folding. Nature 1996;379:96-8.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 118
    • 0345304461 scopus 로고    scopus 로고
    • Origin of unusual φ-values in protein folding: Evidence against specific nucleation sites
    • Sánchez IE, Kiefhaber T. Origin of unusual φ-values in protein folding: evidence against specific nucleation sites. J. Mol. Biol. 2003;334:1077-85.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1077-1085
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 119
    • 0345862295 scopus 로고    scopus 로고
    • Are residues in protein folding nucleus evolutionarily conserved?
    • Tseng YY, Liang J. Are residues in protein folding nucleus evolutionarily conserved?. J. Mol. Biol. 2004;335:869-980.
    • (2004) J. Mol. Biol. , vol.335 , pp. 869-980
    • Tseng, Y.Y.1    Liang, J.2
  • 121
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for unfolding/folding of FKBP12
    • Fulton K, Main E, Daggett V, Jackson SE. Mapping the interactions present in the transition state for unfolding/folding of FKBP12. J. Mol. Biol. 1999;291:445-61.
    • (1999) J. Mol. Biol. , vol.291 , pp. 445-461
    • Fulton, K.1    Main, E.2    Daggett, V.3    Jackson, S.E.4
  • 122
    • 0033015989 scopus 로고    scopus 로고
    • The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    • Kragelund BB, Osmark P, Neergaard TB, Schiodt J, Kristiansen K, Knudsen J, Poulsen FM. The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 1999;6:594-601.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 594-601
    • Kragelund, B.B.1    Osmark, P.2    Neergaard, T.B.3    Schiodt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 123
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
    • Lopez-Hernandez E, Serrano L. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2. Fold. Des. 1996;1:43-55.
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 124
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
    • Grantcharova VP, Riddle DS, Santiago JV, Baker D. Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain. Nat. Struct. Biol. 1998;5:714-20.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 714-720
    • Grantcharova, V.P.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 125
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • Chiti F, Taddei N, White P, Bucciantini M, Magherini F, Stefani M, Dobson C. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 1999;6:1005-9.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.7
  • 126
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • Villegas V, Martinez JC, Aviles FX, Serrano L. Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 1998;283:1027-36.
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 127
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez JC, Serrano L. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 1999;6:1010-6.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 131
    • 0032496419 scopus 로고    scopus 로고
    • Protein folding and protein evolution: Common folding nucleus in different subfamilies of c-type cytochromes?
    • Ptitsyn OB. Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?. J. Mol. Biol. 1998;278:655-66.
    • (1998) J. Mol. Biol. , vol.278 , pp. 655-666
    • Ptitsyn, O.B.1
  • 132
    • 0033588067 scopus 로고    scopus 로고
    • Non-functional conserved residues in globins and their possible role as a folding nucleus
    • Ptitsyn OB, Ting K-L. Non-functional conserved residues in globins and their possible role as a folding nucleus. J. Mol. Biol. 1999;291:671-82.
    • (1999) J. Mol. Biol. , vol.291 , pp. 671-682
    • Ptitsyn, O.B.1    Ting, K.-L.2
  • 133
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding kinetics and function
    • Mirny LA, Shakhnovich EI. Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function. J. Mol. Biol. 1999;291:177-96.
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 136
    • 0035793212 scopus 로고    scopus 로고
    • The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold
    • Cota E, Steward A, Fowler SB, Clarke J. The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold. J. Mol. Biol. 2001;305:1185-94.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1185-1194
    • Cota, E.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 137
    • 0035957514 scopus 로고    scopus 로고
    • Evolutionary conservation of the folding nucleus
    • Mirny L, Shakhnovich E. Evolutionary conservation of the folding nucleus. J. Mol. Biol. 2001;308:123-9.
    • (2001) J. Mol. Biol. , vol.308 , pp. 123-129
    • Mirny, L.1    Shakhnovich, E.2
  • 138
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations
    • Li A, Daggett V. Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations. J. Mol. Biol. 1996;257:412-29.
    • (1996) J. Mol. Biol. , vol.257 , pp. 412-429
    • Li, A.1    Daggett, V.2
  • 139
    • 0029124153 scopus 로고
    • Acid and thermal denaturation of barnase investigated by molecular dynamics simulations
    • Caflisch A, Karplus M. Acid and thermal denaturation of barnase investigated by molecular dynamics simulations. J. Mol. Biol. 1995;252:672-708.
    • (1995) J. Mol. Biol. , vol.252 , pp. 672-708
    • Caflisch, A.1    Karplus, M.2
  • 141
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis T, Karplus M. "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science 1997;278:1928-31.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 142
    • 0345411345 scopus 로고    scopus 로고
    • Hierarchy of structure loss in MD simulations of src SH3 domain unfolding
    • Isai J, Levitt M, Baker D. Hierarchy of structure loss in MD simulations of src SH3 domain unfolding. J. Mol. Biol. 1999;291:215-25.
    • (1999) J. Mol. Biol. , vol.291 , pp. 215-225
    • Isai, J.1    Levitt, M.2    Baker, D.3
  • 143
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V, Fersht AR. The present view of the mechanism of protein folding. Nat. Rev. Mol. Cell Biol. 2003;4:497-502.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.R.2
  • 144
    • 0030775114 scopus 로고    scopus 로고
    • Can protein unfolding simulate protein folding?
    • Finkelstein AV. Can protein unfolding simulate protein folding?. Protein Eng. 1997;10:843-5.
    • (1997) Protein Eng. , vol.10 , pp. 843-845
    • Finkelstein, A.V.1
  • 145
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • Mayor U, Johnson CM, Daggett V, Fersht AR. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl. Acad. Sci. USA 2000;97:13518-22.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fersht, A.R.4
  • 149
    • 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;4:10-9.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 150
    • 0033574069 scopus 로고    scopus 로고
    • Folding pathway of a lattice model for proteins
    • Pande VS, Rocksar DS. Folding pathway of a lattice model for proteins. Proc. Natl. Acad. Sci. USA 1999;96:1273-8.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1273-1278
    • Pande, V.S.1    Rocksar, D.S.2
  • 151
    • 0033515615 scopus 로고    scopus 로고
    • Exploring structures in protein folding funnels with free energy functionals: The transition state ensemble
    • Shoemaker BA, Wang J, Wolynes PG. Exploring structures in protein folding funnels with free energy functionals: the transition state ensemble. J. Mol. Biol. 1999;287:675-94.
    • (1999) J. Mol. Biol. , vol.287 , pp. 675-694
    • Shoemaker, B.A.1    Wang, J.2    Wolynes, P.G.3
  • 152
    • 0033515614 scopus 로고    scopus 로고
    • Exploring structures in protein folding funnels with free energy functionals: The denatured ensemble
    • Shoemaker BA, Wolynes PG. Exploring structures in protein folding funnels with free energy functionals: the denatured ensemble. J. Mol. Biol. 1999;287:657-74.
    • (1999) J. Mol. Biol. , vol.287 , pp. 657-674
    • Shoemaker, B.A.1    Wolynes, P.G.2
  • 153
    • 0034612228 scopus 로고    scopus 로고
    • Investigation of routes and funnels in protein folding by free energy functional methods
    • Plotkin SS, Onuchic JN. Investigation of routes and funnels in protein folding by free energy functional methods. Proc. Natl. Acad. Sci. USA 2000;97:6509-14.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6509-6514
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 154
    • 0033613131 scopus 로고    scopus 로고
    • A theoretical search for folding/unfolding nuclei in three-dimensional protein structures
    • Galzitskaya OV, Finkelstein AV. A theoretical search for folding/unfolding nuclei in three-dimensional protein structures. Proc. Natl. Acad. Sci. USA 1999;96:11299-304.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11299-11304
    • Galzitskaya, O.V.1    Finkelstein, A.V.2
  • 155
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures
    • Alm E, Baker D. Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures. Proc. Natl. Acad. Sci. USA 1999;96:11305-10.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 156
    • 0033613165 scopus 로고    scopus 로고
    • A simple model for calculating the kinetics of protein folding from three-dimensional structures
    • Munõz V, Eaton WA. A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc. Natl. Acad. Sci. USA 1999;96:11311-6.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11311-11316
    • Munõz, V.1    Eaton, W.A.2
  • 157
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi H, Ueda Y, Gô N. Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions. Int. J. Pept. Prot. Res. 1975;7:445-59.
    • (1975) Int. J. Pept. Prot. Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Gô, N.3
  • 158
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D. A surprising simplicity to protein folding. Nature 2000;405:39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 159
    • 0032742688 scopus 로고    scopus 로고
    • Gö-ing for the prediction of protein folding mechanisms
    • Takada S. Gö-ing for the prediction of protein folding mechanisms. Proc. Natl. Acad. Sci. USA 1999;96:11698-700.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11698-11700
    • Takada, S.1
  • 160
    • 0036384269 scopus 로고    scopus 로고
    • Simple physical models connect theory and experiment in protein folding kinetics
    • Alm E, Morozov AV, Kortemme T, Baker D. Simple physical models connect theory and experiment in protein folding kinetics. J. Mol. Biol. 2002;322:463-76.
    • (2002) J. Mol. Biol. , vol.322 , pp. 463-476
    • Alm, E.1    Morozov, A.V.2    Kortemme, T.3    Baker, D.4
  • 162
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta
    • Clementi C, Jennings PA, Onuchic JN. How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta. Proc. Natl. Acad. Sci. USA 2000;97:5871-6.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 163
    • 0036562160 scopus 로고    scopus 로고
    • Sensitivity of folding pathway to the details of amino-acid sequence
    • Galzitskaya OV. Sensitivity of folding pathway to the details of amino-acid sequence. Mol. Biol. (Moscow) 2002;36:386-90.
    • (2002) Mol. Biol. (Moscow) , vol.36 , pp. 386-390
    • Galzitskaya, O.V.1
  • 164
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of beta-hairpin formation in protein G folding
    • McCallister EL, Alm E, Baker D. Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 2000;7:669-73.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 165
    • 0031486612 scopus 로고    scopus 로고
    • Physical reasons for a rapid folding of stable protein structures: A solution of Levinthal's paradox
    • (Russia, Eng. Edition)
    • Finkelstein AV, Badretdinov AYa. Physical reasons for a rapid folding of stable protein structures: a solution of Levinthal's paradox. Mol. Biol. (Russia, Eng. Edition) 1997;31:391-8.
    • (1997) Mol. Biol. , vol.31 , pp. 391-398
    • Finkelstein, A.V.1    Badretdinov, A.Ya.2
  • 166
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Go-like model
    • Koga N, Takada S. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model. J. Mol. Biol. 2001;313:171-80.
    • (2001) J. Mol. Biol. , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 167
    • 85030887500 scopus 로고    scopus 로고
    • Thermal denaturation and folding rates of single domain proteins: Size matters, Polymers
    • Submitted
    • Li MS, Klimov DK, Thirumalai D. Thermal denaturation and folding rates of single domain proteins: size matters, Polymers. Submitted.
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 168
    • 85030876806 scopus 로고    scopus 로고
    • Prediction of protein folding rates from the amino-acid sequence-predicted secondary structure
    • Submitted
    • Ivankov DN, Finkelstein AV, Prediction of protein folding rates from the amino-acid sequence-predicted secondary structure. Proc. Natl. Acad. Sci. USA. Submitted.
    • Proc. Natl. Acad. Sci. USA.
    • Ivankov, D.N.1    Finkelstein, A.V.2
  • 169
    • 0037402639 scopus 로고    scopus 로고
    • Chain length is the most important determinant of protein folding with three-state kinetics
    • Galzitskaya OV, Garbuzynskiy SO, Ivankov DN, Finkelstein AV. Chain length is the most important determinant of protein folding with three-state kinetics. Proteins 2003;51:162-6.
    • (2003) Proteins , vol.51 , pp. 162-166
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Ivankov, D.N.3    Finkelstein, A.V.4
  • 170
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht AR. Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl. Acad. Sci. USA 2000;97:1525-9.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 171
    • 0037566828 scopus 로고    scopus 로고
    • A simple parameter relating sequences with folding rates of small alpha helical proteins
    • Shao H, Peng Y, Zeng Z-H. A simple parameter relating sequences with folding rates of small alpha helical proteins. Protein Peptide Lett. 2003;10:277-80.
    • (2003) Protein Peptide Lett. , vol.10 , pp. 277-280
    • Shao, H.1    Peng, Y.2    Zeng, Z.-H.3
  • 172
    • 0038047129 scopus 로고    scopus 로고
    • Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding
    • Calloni G, Taddei N, Plaxco KW, Ramponi G, Stefani M, Chiti F. Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 2003;330:577-91.
    • (2003) J. Mol. Biol. , vol.330 , pp. 577-591
    • Calloni, G.1    Taddei, N.2    Plaxco, K.W.3    Ramponi, G.4    Stefani, M.5    Chiti, F.6
  • 173
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 1999;292:195-202. http://www.psipred.net/.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 174
    • 0025398721 scopus 로고
    • WHAT IF - A molecular modeling and drug design program
    • Vriend G. WHAT IF - a molecular modeling and drug design program. J. Mol. Graphics 1990;8:52-6.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1


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