메뉴 건너뛰기




Volumn 30, Issue 1, 1998, Pages 2-33

Protein folding in the landscape perspective: Chevron plots and non- rrhenius kinetics

Author keywords

Chevron plot; Energy landscape; Folding funnel; Kinetic trap; Lattice models; Non Arrhenius behavior

Indexed keywords

ARTICLE; ENTROPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DETERMINATION; PROTEIN FOLDING; TEMPERATURE MEASUREMENT;

EID: 0003166498     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<2::AID-PROT2>3.0.CO;2-R     Document Type: Article
Times cited : (426)

References (197)
  • 1
    • 0028776642 scopus 로고
    • Matching speed and stability
    • Baldwin, R.L. Matching speed and stability. Nature 369: 183-184, 1994.
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 2
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R.L. The nature of protein folding pathways: The classical versus the new view. J. Biomol. NMR 5:103-109, 1995.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 5
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M., Šali, A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:58-73, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Šali, A.2
  • 7
    • 0001103473 scopus 로고    scopus 로고
    • Kinetics of folding of proteins and RNA
    • Thirumalai, D., Woodson, S.A. Kinetics of folding of proteins and RNA. Acc. Chem. Res. 29:433-439, 1996.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 433-439
    • Thirumalai, D.1    Woodson, S.A.2
  • 8
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., Chan, H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19, 1997.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 9
    • 67349189383 scopus 로고
    • The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
    • Anfinsen, C.B., Haber, E., Sela, M., White, F.H., Jr. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl. Acad. Sci. USA 47:1309-1314, 1961.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1309-1314
    • Anfinsen, C.B.1    Haber, E.2    Sela, M.3    White Jr., F.H.4
  • 10
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. Principles that govern the folding of protein chains. Science 181:223-230, 1973.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 11
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. Are there pathways for protein folding? J. Chim. Phys. 65:44-45, 1968.
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 13
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K.A. Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509, 1985.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 15
    • 0343368213 scopus 로고
    • The stabilities of globular proteins
    • Oxender, D.L., Fox, C.F. (eds.). New York: Alan R. Liss, Inc.
    • Dill, K.A. The stabilities of globular proteins. In: "Protein Engineering." Oxender, D.L., Fox, C.F. (eds.). New York: Alan R. Liss, Inc., 1987:187-192.
    • (1987) Protein Engineering , pp. 187-192
    • Dill, K.A.1
  • 16
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P.E., Montal, M., Onuchic, J.N. Protein folding funnels: A kinetic approach to the sequence-structure relationship. Proc. Natl. Acad. Sci. USA 89:8721-8725, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 17
    • 0015220649 scopus 로고
    • Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins
    • Ikai, A., Tanford, C. Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins. Nature 230:100-102, 1971.
    • (1971) Nature , vol.230 , pp. 100-102
    • Ikai, A.1    Tanford, C.2
  • 18
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins. I. Mathematical analysis
    • Ikai, A., Tanford, C. Kinetics of unfolding and refolding of proteins. I. Mathematical analysis. J. Mol. Biol. 73:145-163, 1973.
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2
  • 19
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c
    • Ikai, A., Fish, W.W., Tanford, C. Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c. J. Mol. Biol. 73:165-184, 1973.
    • (1973) J. Mol. Biol. , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 20
    • 0015918873 scopus 로고
    • Kinetics of unfolding and refolding of proteins. III. Results for lysozyme
    • Tanford, C., Aune, K.C., Ikai, A. Kinetics of unfolding and refolding of proteins. III. Results for lysozyme. J. Mol. Biol. 73:185-197, 1973.
    • (1973) J. Mol. Biol. , vol.73 , pp. 185-197
    • Tanford, C.1    Aune, K.C.2    Ikai, A.3
  • 21
    • 0015155644 scopus 로고
    • The sequential unfolding of ribonuclease A: Detection of a fast initial phase in the kinetics of unfolding
    • Tsong, T.Y., Baldwin, R.L., Elson, E.L. The sequential unfolding of ribonuclease A: Detection of a fast initial phase in the kinetics of unfolding. Proc. Natl. Acad. Sci. USA 68:2712-2715, 1971.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2712-2715
    • Tsong, T.Y.1    Baldwin, R.L.2    Elson, E.L.3
  • 22
    • 0015375693 scopus 로고
    • Properties of the refolding and unfolding reactions of ribonuclease A
    • Tsong, T.Y., Baldwin, R.L., Elson, E.L. Properties of the refolding and unfolding reactions of ribonuclease A. Proc. Natl. Acad. Sci. USA 69:1809-1812, 1972.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1809-1812
    • Tsong, T.Y.1    Baldwin, R.L.2    Elson, E.L.3
  • 23
    • 0015505381 scopus 로고
    • A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A
    • Tsong, T.Y., Baldwin, R.L., McPhie, P., Elson, E.L. A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A. J. Mol. Biol. 63:453-475, 1972.
    • (1972) J. Mol. Biol. , vol.63 , pp. 453-475
    • Tsong, T.Y.1    Baldwin, R.L.2    McPhie, P.3    Elson, E.L.4
  • 24
    • 0015793989 scopus 로고
    • Detection of three kinetic phases in the thermal unfolding of ferricytochrome c
    • Tsong, T.Y. Detection of three kinetic phases in the thermal unfolding of ferricytochrome c. Biochemistry 12:2209-2214, 1973.
    • (1973) Biochemistry , vol.12 , pp. 2209-2214
    • Tsong, T.Y.1
  • 25
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J.D., Wolynes, P.G. Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA 84:7524-7528, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 26
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model with applications to protein folding
    • Bryngelson, J.D., Wolynes, P.G. Intermediates and barrier crossing in a random energy model with applications to protein folding. J. Phys. Chem. 93:6902-6915, 1989.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 27
    • 36549094651 scopus 로고
    • Intrachain loops in polymers: Effects of excluded volume
    • Erratum. J. Chem. Phys. 96:3361, 1992
    • Chan, H.S., Dill, K.A. Intrachain loops in polymers: Effects of excluded volume. J. Chem. Phys. 90:492-509, 1989. Erratum. J. Chem. Phys. 96:3361, 1992.
    • (1989) J. Chem. Phys. , vol.90 , pp. 492-509
    • Chan, H.S.1    Dill, K.A.2
  • 29
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • Lau, K.F., Dill, K.A. A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules 22:3986-3997, 1989.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 31
    • 0343274684 scopus 로고    scopus 로고
    • Solvation: How to obtain microscopic energies from partitioning and solvation experiments
    • Chan, H.S., Dill, K.A. Solvation: How to obtain microscopic energies from partitioning and solvation experiments. Annu. Rev. Biophys. Biomol. Struct. 26:425-459, 1997.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 425-459
    • Chan, H.S.1    Dill, K.A.2
  • 34
    • 0026643094 scopus 로고
    • The nature of folded states of globular proteins
    • Honeycutt, J.D., Thirumalai, D. The nature of folded states of globular proteins. Biopolymers 32:695-709, 1992.
    • (1992) Biopolymers , vol.32 , pp. 695-709
    • Honeycutt, J.D.1    Thirumalai, D.2
  • 35
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho, C.J., Thirumalai, D. Kinetics and thermodynamics of folding in model proteins. Proc. Natl. Acad. Sci. USA 90:6369-6372, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 37
    • 36449008575 scopus 로고
    • Energy landscape and the collapse dynamics of homopolymers
    • Chan, H.S., Dill, K.A. Energy landscape and the collapse dynamics of homopolymers. J. Chem. Phys. 99:2116-2127, 1993.
    • (1993) J. Chem. Phys. , vol.99 , pp. 2116-2127
    • Chan, H.S.1    Dill, K.A.2
  • 38
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H.S., Dill, K.A. Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100: 9238-9257, 1994.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 39
    • 0007725036 scopus 로고
    • Folding kinetics of protein-like heteropolymers
    • Socci, N.D., Onuchic, J.N. Folding kinetics of protein-like heteropolymers. J. Chem. Phys. 101:1519-1528, 1994.
    • (1994) J. Chem. Phys. , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 40
    • 36448999595 scopus 로고
    • Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice model simulations
    • Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I. Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice model simulations. J. Chem. Phys. 101:6052-6062, 1994.
    • (1994) J. Chem. Phys. , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 42
    • 0028835443 scopus 로고
    • Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labeling experiments
    • Thirumalai, D., Guo, Z. Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labeling experiments. Biopolymers 35:137-140, 1995.
    • (1995) Biopolymers , vol.35 , pp. 137-140
    • Thirumalai, D.1    Guo, Z.2
  • 43
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Guo, Z., Thirumalai, D. Kinetics of protein folding: Nucleation mechanism, time scales, and pathways. Biopolymers 36:83-102, 1995.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 44
    • 0029563457 scopus 로고
    • Folding of chains with random and edited sequences: Similarities and differences
    • Galzitskaya, O.V., Finkelstein, A.V. Folding of chains with random and edited sequences: Similarities and differences. Protein Eng. 8:883-892, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 883-892
    • Galzitskaya, O.V.1    Finkelstein, A.V.2
  • 45
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • Zwanzig, R. Simple model of protein folding kinetics. Proc. Natl. Acad. Sci. USA 92:9801-9804, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 46
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • Veitshans, T., Klimov, D., Thirumalai, D. Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties. Folding Design 2:1-22, 1997.
    • (1997) Folding Design , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.2    Thirumalai, D.3
  • 47
    • 6844224617 scopus 로고    scopus 로고
    • Nucleation-collapse process in protein folding: Evidence for the nonuniqueness of the folding nucleus
    • In press
    • Guo, Z., Thirumalai, D. Nucleation-collapse process in protein folding: Evidence for the nonuniqueness of the folding nucleus. Folding & Design. (In press.)
    • Folding & Design
    • Guo, Z.1    Thirumalai, D.2
  • 48
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I. Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 252:460-471, 1995.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 49
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I. Specific nucleus as the transition state for protein folding: Evidence from the lattice model. Biochemistry 33:10026-10036, 1994.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 50
    • 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 379:96-98, 1996.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 51
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • France
    • Thirumalai, D. From minimal models to real proteins: Time scales for protein folding kinetics. J. Physique. I (France) 5:1457-1467, 1995.
    • (1995) J. Physique. I , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 53
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S.E., Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30:10428-10435, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 54
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • Jackson, S.E., Fersht, A.R. Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry 30:10436-10443, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 56
    • 0028935887 scopus 로고
    • Structure and stability of monomeric λ repressor: NMR evidence for two-state folding
    • Huang, G.S., Oas, T.G. Structure and stability of monomeric λ repressor: NMR evidence for two-state folding. Biochemistry 34:3884-3892, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 57
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • Huang, G.S., Oas, T.G. Submillisecond folding of monomeric λ repressor. Proc. Natl. Acad. Sci. USA 92:6878-6882, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 58
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T.R., Mayne, L., Englander, S.W. Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins Struct. Funct. Genet. 24:413-426, 1996.
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 60
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber, T. Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA 92:9029-9033, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 61
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler, T., Schmid, F.X. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry 35:16833-16842, 1996.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 62
  • 63
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. Protein denaturation. Adv. Protein Chem. 23:121-282, 1968.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 64
    • 0021103614 scopus 로고
    • Effects of a single amino acid substitution on the folding of the α-subunit of tryptophan synthase
    • Matthews C.R., Crisanti, M.M., Manz, J.T., Gepner, G.L. Effects of a single amino acid substitution on the folding of the α-subunit of tryptophan synthase. Biochemistry 22: 1445-1452, 1983.
    • (1983) Biochemistry , vol.22 , pp. 1445-1452
    • Matthews, C.R.1    Crisanti, M.M.2    Manz, J.T.3    Gepner, G.L.4
  • 65
    • 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 23:2473-2488, 1984.
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.-I.1    Sugihara, M.2
  • 66
    • 0023517017 scopus 로고
    • Effects of point mutations on the folding of globular proteins
    • Matthews, C.R. Effects of point mutations on the folding of globular proteins. Methods Enzymol. 154:498-511, 1987.
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 67
    • 0023358977 scopus 로고
    • Mutant sequences as probes of protein folding mechanisms
    • Matthews, C.R., Hurle, M.R. Mutant sequences as probes of protein folding mechanisms. BioEssays 6:254-257, 1987.
    • (1987) BioEssays , vol.6 , pp. 254-257
    • Matthews, C.R.1    Hurle, M.R.2
  • 69
    • 0024977331 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies
    • Chen, B.-L., Schellman, J.A. Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. Biochemistry 28:685-691, 1989.
    • (1989) Biochemistry , vol.28 , pp. 685-691
    • Chen, B.-L.1    Schellman, J.A.2
  • 70
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen, B.-L., Baase, W.A., Schellman, J.A. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28:691-699, 1989.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.-L.1    Baase, W.A.2    Schellman, J.A.3
  • 71
    • 0026545583 scopus 로고
    • Folding kinetics of T4 lysozyme and nine mutants at 12°C
    • Chen, B.-L., Baase, W.A., Nicholson, H., Schellman, J.A. Folding kinetics of T4 lysozyme and nine mutants at 12°C. Biochemistry 31:1464-1476, 1992.
    • (1992) Biochemistry , vol.31 , pp. 1464-1476
    • Chen, B.-L.1    Baase, W.A.2    Nicholson, H.3    Schellman, J.A.4
  • 72
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C.R. Pathways of protein folding. Annu. Rev. Biochem. 62:653-683, 1993.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 73
    • 0028271856 scopus 로고
    • Thermodynamic properties of the transition state for the rate-limiting step in the folding of the a subunit of tryptophan synthase
    • Chen, X., Matthews, C.R. Thermodynamic properties of the transition state for the rate-limiting step in the folding of the a subunit of tryptophan synthase. Biochemistry 33:6356-6362, 1994.
    • (1994) Biochemistry , vol.33 , pp. 6356-6362
    • Chen, X.1    Matthews, C.R.2
  • 75
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A.R. Characterizing transition states in protein folding: An essential step in the puzzle. Curr. Opin. Struct. Biol. 5:79-84, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 76
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg, M., Tan, Y.-J., Fersht, A.R. Negative activation enthalpies in the kinetics of protein folding. Proc. Natl. Acad. Sci. USA 92:8926-8929, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.-J.2    Fersht, A.R.3
  • 77
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan, Y.-J., Oliveberg, M., Fersht, A.R. Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264:377-389, 1996.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.-J.1    Oliveberg, M.2    Fersht, A.R.3
  • 78
    • 0025906282 scopus 로고
    • Polymer principles in protein structure and stability
    • Chan, H.S., Dill, K.A. Polymer principles in protein structure and stability. Annu. Rev. Biophys. Biophys. Chem. 20:447-490, 1991.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 447-490
    • Chan, H.S.1    Dill, K.A.2
  • 79
    • 33744825406 scopus 로고
    • "Sequence space soup" of proteins and copolymers
    • Chan, H.S., Dill, K.A. "Sequence space soup" of proteins and copolymers. J. Chem. Phys. 95:3775-3787, 1991.
    • (1991) J. Chem. Phys. , vol.95 , pp. 3775-3787
    • Chan, H.S.1    Dill, K.A.2
  • 80
    • 0000868733 scopus 로고
    • The protein folding problem
    • February
    • Chan, H.S., Dill, K.A. The protein folding problem. Physics Today 46:24-32, February 1993.
    • (1993) Physics Today , vol.46 , pp. 24-32
    • Chan, H.S.1    Dill, K.A.2
  • 81
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • Chan, H.S., Dill, K.A. A simple model of chaperonin-mediated protein folding. Proteins Struct. Funct. Genet. 24:345-351, 1996.
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 82
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique
    • Socci, N.D., Onuchic, J.N. Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique. J. Chem. Phys. 103:4732-4744, 1995.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 83
    • 0028466392 scopus 로고
    • The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
    • Okazaki, A., Ikura, T., Nikaido, K., Kuwajima, K. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nat. Struct. Biol. 1:439-446, 1994.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 439-446
    • Okazaki, A.1    Ikura, T.2    Nikaido, K.3    Kuwajima, K.4
  • 85
    • 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., Gō, 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. 7:445-459, 1975.
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 86
    • 0000355428 scopus 로고
    • Respective roles of short- and long-range interactions in protein folding
    • Gō, N., Taketomi, H. Respective roles of short- and long-range interactions in protein folding. Proc. Natl. Acad. Sci. USA 75:559-563, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 559-563
    • Go, N.1    Taketomi, H.2
  • 87
    • 0019571422 scopus 로고
    • Noninteracting local-structure model of folding and unfolding transition in globular proteins. II. Application to two-dimensional lattice proteins
    • Abe, H., Gō, N. Noninteracting local-structure model of folding and unfolding transition in globular proteins. II. Application to two-dimensional lattice proteins. Biopolymers 20:1013-1031, 1981.
    • (1981) Biopolymers , vol.20 , pp. 1013-1031
    • Abe, H.1    Go, N.2
  • 88
    • 0029289336 scopus 로고
    • Computer simulation studies of protein refolding pathways and intermediates
    • Gupta, P., Hall, C.K. Computer simulation studies of protein refolding pathways and intermediates. Am. Inst. Chem. Eng. J. 41:985-990, 1995.
    • (1995) Am. Inst. Chem. Eng. J. , vol.41 , pp. 985-990
    • Gupta, P.1    Hall, C.K.2
  • 89
    • 0019569599 scopus 로고
    • Noninteracting local-structure model of folding and unfolding transition in globular proteins. I. Formulation
    • Gō, N., Abe, H. Noninteracting local-structure model of folding and unfolding transition in globular proteins. I. Formulation. Biopolymers 20:991-1011, 1981.
    • (1981) Biopolymers , vol.20 , pp. 991-1011
    • Go, N.1    Abe, H.2
  • 90
    • 0000669827 scopus 로고
    • Monte Carlo simulation of folding transitions of simple model proteins using a chain growth algorithm
    • O'Toole, E.M., Panagiotopoulos, A.Z. Monte Carlo simulation of folding transitions of simple model proteins using a chain growth algorithm. J. Chem. Phys. 97:8644-8652, 1992.
    • (1992) J. Chem. Phys. , vol.97 , pp. 8644-8652
    • O'Toole, E.M.1    Panagiotopoulos, A.Z.2
  • 91
    • 0010801118 scopus 로고
    • Effect of sequence and intermolecular interactions on the number and nature of low-energy states for simple model proteins
    • O'Toole, E.M., Panagiotopoulos, A.Z. Effect of sequence and intermolecular interactions on the number and nature of low-energy states for simple model proteins. J. Chem. Phys. 98:3185-3190, 1993.
    • (1993) J. Chem. Phys. , vol.98 , pp. 3185-3190
    • O'Toole, E.M.1    Panagiotopoulos, A.Z.2
  • 92
    • 0000515198 scopus 로고
    • Monte Carlo simulation of a first-order transition for protein folding
    • Hao, M.-H., Scheraga, H.A. Monte Carlo simulation of a first-order transition for protein folding. J. Phys. Chem. 98:4940-4948, 1994.
    • (1994) J. Phys. Chem. , vol.98 , pp. 4940-4948
    • Hao, M.-H.1    Scheraga, H.A.2
  • 93
    • 33751158061 scopus 로고
    • Statistical thermodynamics of protein folding: Sequence dependence
    • Hao, M.-H., Scheraga, H.A. Statistical thermodynamics of protein folding: Sequence dependence. J. Phys. Chem. 98:9882-9893, 1994.
    • (1994) J. Phys. Chem. , vol.98 , pp. 9882-9893
    • Hao, M.-H.1    Scheraga, H.A.2
  • 94
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin, A.M., Abkevich, V.I., Shakhnovich, E.I. Is burst hydrophobic collapse necessary for protein folding? Biochemistry 34:3066-3076, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 96
    • 0030604696 scopus 로고    scopus 로고
    • Local interactions dominate folding in a simple protein model
    • Unger, R., Moult, J. Local interactions dominate folding in a simple protein model, J. Mol. Biol. 259:988-994, 1996.
    • (1996) J. Mol. Biol. , vol.259 , pp. 988-994
    • Unger, R.1    Moult, J.2
  • 97
    • 0029945395 scopus 로고    scopus 로고
    • How optimization of potential functions affects protein folding
    • Hao, M.-H., Scheraga, H.A. How optimization of potential functions affects protein folding. Proc. Natl. Acad. Sci. USA 93:4984-4989, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4984-4989
    • Hao, M.-H.1    Scheraga, H.A.2
  • 98
    • 0029554952 scopus 로고
    • Designing amino acid sequences to fold with good hydrophobic cores
    • Sun, S., Brem, R., Chan, H.S., Dill, K.A. Designing amino acid sequences to fold with good hydrophobic cores. Protein Eng. 8:1205-1213, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 1205-1213
    • Sun, S.1    Brem, R.2    Chan, H.S.3    Dill, K.A.4
  • 99
    • 0003155594 scopus 로고    scopus 로고
    • Comparing folding codes for proteins and polymers
    • Chan, H.S., Dill, K.A. Comparing folding codes for proteins and polymers. Proteins Struct. Funct. Genet. 24:335-344, 1996,
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 335-344
    • Chan, H.S.1    Dill, K.A.2
  • 100
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • Šali, A., Shakhnovich, E., Karplus, M. Kinetics of protein folding: A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235:1614-1636, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Šali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 102
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Erratum. Phys. Rev. Lett. 74:2618, 1995
    • Shakhnovich, E.I. Proteins with selected sequences fold into unique native conformation. Phys. Rev. Lett. 72:3907-3910, 1994. Erratum. Phys. Rev. Lett. 74:2618, 1995.
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 103
    • 0025146274 scopus 로고
    • Implications of thermodynamics of protein folding for evolution of primary sequences
    • Shakhnovich, E.I., Gutin, A.M. Implications of thermodynamics of protein folding for evolution of primary sequences. Nature 346:773-775, 1990.
    • (1990) Nature , vol.346 , pp. 773-775
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 104
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō, N. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12:183-210, 1983.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 105
    • 0030628053 scopus 로고    scopus 로고
    • On the theory of folding kinetics for short proteins
    • Pande, V.S., Grosberg, A. Yu., Tanaka, T. On the theory of folding kinetics for short proteins. Folding Design 2:109-114, 1997.
    • (1997) Folding Design , vol.2 , pp. 109-114
    • Pande, V.S.1    Grosberg, A.Yu.2    Tanaka, T.3
  • 106
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N.D., Onuchic, J.N., Wolynes, P.G. Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104:5860-5868, 1996.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 108
    • 36049060531 scopus 로고
    • Diffusion constants near the critical point for time-dependent Ising models. I
    • Kawasaki, K. Diffusion constants near the critical point for time-dependent Ising models. I. Phys. Rev. 145:224-230, 1966.
    • (1966) Phys. Rev. , vol.145 , pp. 224-230
    • Kawasaki, K.1
  • 110
    • 4243572706 scopus 로고    scopus 로고
    • A criterion that determines the foldability of proteins
    • Klimov, D.K., Thirumalai, D. A criterion that determines the foldability of proteins. Phys. Rev. Lett. 76:4070-4073, 1996.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 4070-4073
    • Klimov, D.K.1    Thirumalai, D.2
  • 113
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S., Baldwin, R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:459-489, 1982.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 114
    • 0021113912 scopus 로고
    • Mechanism of folding ribonuclease A. Slow refolding is a sequential reaction via structural intermediates
    • Schmid, F.X. Mechanism of folding ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry 22:4690-4696, 1983.
    • (1983) Biochemistry , vol.22 , pp. 4690-4696
    • Schmid, F.X.1
  • 115
    • 0028929204 scopus 로고
    • Kinetics of protein folding
    • Chan, H.S. Kinetics of protein folding. Nature 373:664-665, 1995.
    • (1995) Nature , vol.373 , pp. 664-665
    • Chan, H.S.1
  • 116
    • 0029028698 scopus 로고
    • Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways
    • Camacho, C.J., Thirumalai, D. Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways. Proteins Struct. Funct. Genet. 22:27-40, 1995.
    • (1995) Proteins Struct. Funct. Genet. , vol.22 , pp. 27-40
    • Camacho, C.J.1    Thirumalai, D.2
  • 117
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S.E., Dobson, C.M., Evans, P.A., The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358:302-307, 1992.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 118
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson, C.M., Evans, P.A., Radford, S.E. Understanding how proteins fold: The lysozyme story so far. Trends Biochem Sci. 19:31-37, 1994.
    • (1994) Trends Biochem Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 119
    • 0000846782 scopus 로고
    • Effect of rotation on the diffusion-controlled rate of ligand-protein association
    • Hill, T.L. Effect of rotation on the diffusion-controlled rate of ligand-protein association. Proc. Natl. Acad. Sci. USA 72:4918-4922, 1975.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4918-4922
    • Hill, T.L.1
  • 120
    • 0016927165 scopus 로고
    • Diffusion frequency factors in some simple examples of transition-state rate theory
    • Hill, T.L. Diffusion frequency factors in some simple examples of transition-state rate theory. Proc. Natl. Acad. Sci. USA 73:679-683, 1976.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 679-683
    • Hill, T.L.1
  • 121
    • 0001554628 scopus 로고
    • A rate process with an entropy barrier
    • Zhou, H.-X., Zwanzig, R. A rate process with an entropy barrier. J. Chem. Phys. 94:6147-6152, 1991.
    • (1991) J. Chem. Phys. , vol.94 , pp. 6147-6152
    • Zhou, H.-X.1    Zwanzig, R.2
  • 122
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman, C.M., Loskutoff, D.J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J. Biol. Chem. 260:11581-11587, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 123
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Erratum Nature 364:737, 1993
    • Carrell, R.W., Evans, D.L., Stein, P.E. Mobile reactive centre of serpins and the control of thrombosis. Nature 353:576-578, 1991. Erratum Nature 364:737, 1993.
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.E.3
  • 125
    • 0030475698 scopus 로고    scopus 로고
    • Kinetically controlled folding of the serpin plasminogen activator inhibitor 1
    • Wang, Z., Mottonen, J., Goldsmith, E.J. Kinetically controlled folding of the serpin plasminogen activator inhibitor 1. Biochemistry 35:16443-16448, 1996.
    • (1996) Biochemistry , vol.35 , pp. 16443-16448
    • Wang, Z.1    Mottonen, J.2    Goldsmith, E.J.3
  • 127
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J.F., Halvorson, H.R., Brennan, M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14:4953-4963, 1975.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 128
    • 0018132548 scopus 로고
    • Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: A kinetic study of carp parvalbumins
    • Lin, L.-N., Brandts, J.F. Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: A kinetic study of carp parvalbumins. Biochemistry 17:4102-4110, 1978.
    • (1978) Biochemistry , vol.17 , pp. 4102-4110
    • Lin, L.-N.1    Brandts, J.F.2
  • 129
    • 0018143763 scopus 로고
    • Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization
    • Schmid, F.X., Baldwin, R.L. Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization. Proc. Natl. Acad. Sci. USA 75:4764-4768, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4764-4768
    • Schmid, F.X.1    Baldwin, R.L.2
  • 130
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S., Baldwin, R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660, 1990.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 131
    • 0001849773 scopus 로고
    • Proline isomerization as a rate-limiting step
    • Pain, R.H. (ed.). New York: Oxford University Press
    • Nail, B.T. Proline isomerization as a rate-limiting step. In: "Mechanisms of Protein Folding." Pain, R.H. (ed.). New York: Oxford University Press, 1994:80-103.
    • (1994) Mechanisms of Protein Folding , pp. 80-103
    • Nail, B.T.1
  • 132
    • 0017344076 scopus 로고
    • Kinetic analysis of the reversible folding reactions of small proteins: Application to the folding of lysozyme and cytochrome c
    • Hagerman, P.L. Kinetic analysis of the reversible folding reactions of small proteins: Application to the folding of lysozyme and cytochrome c. Biopolymers 16:731-747, 1977.
    • (1977) Biopolymers , vol.16 , pp. 731-747
    • Hagerman, P.L.1
  • 133
    • 0019883235 scopus 로고
    • Nature of the fast and slow refolding reactions of iron(III) cytochrome c
    • Ridge, J.A., Baldwin, R.L., Labhardt, A.M. Nature of the fast and slow refolding reactions of iron(III) cytochrome c. Biochemistry 20:1622-1630, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1622-1630
    • Ridge, J.A.1    Baldwin, R.L.2    Labhardt, A.M.3
  • 135
    • 0026091723 scopus 로고
    • Effects of proline mutations on the unfolding and refolding of human lysozyme: The slow refolding kinetic phase does not result from proline cis-trans isomerization
    • Herning, T., Yutani, K. Taniyama, Y., Kikuchi, M. Effects of proline mutations on the unfolding and refolding of human lysozyme: The slow refolding kinetic phase does not result from proline cis-trans isomerization. Biochemistry 30:9882-9891, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9882-9891
    • Herning, T.1    Yutani, K.2    Taniyama, Y.3    Kikuchi, M.4
  • 136
    • 0026584375 scopus 로고
    • Folding of RNase T1 is decelerated by a specific tertiary contact in the folding intermediate
    • Kiefhaber, T., Grunert, H.-P., Hahn, U., Schmid, F.X. Folding of RNase T1 is decelerated by a specific tertiary contact in the folding intermediate. Proteins Struct. Funct. Genet. 12:171-179, 1992.
    • (1992) Proteins Struct. Funct. Genet. , vol.12 , pp. 171-179
    • Kiefhaber, T.1    Grunert, H.-P.2    Hahn, U.3    Schmid, F.X.4
  • 137
    • 0028402735 scopus 로고
    • The energetic ups and downs of protein folding
    • Creighton, T.E. The energetic ups and downs of protein folding. Nat. Struct. Biol. 1:135-138, 1994.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 135-138
    • Creighton, T.E.1
  • 138
    • 0028810468 scopus 로고
    • Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase
    • Mann, C.J., Shao, X., Matthews, C.R. Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry 34:14573-14580, 1995.
    • (1995) Biochemistry , vol.34 , pp. 14573-14580
    • Mann, C.J.1    Shao, X.2    Matthews, C.R.3
  • 139
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima, K., Hiraoka, Y., Ikeguchi, M., Sugai, S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24:874-881, 1985.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 140
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • Ikeguchi, M., Kuwajima, K., Mitani, M., Sugai, S. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25:6965-6972, 1986.
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 142
    • 0029100019 scopus 로고
    • Watching protein folding unfold
    • Roder, H. Watching protein folding unfold. Nat. Struct. Biol. 2:817-820, 1995.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 817-820
    • Roder, H.1
  • 143
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet. 6:87-103, 1989.
    • (1989) Proteins Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 144
    • 0027394285 scopus 로고
    • Pulsed H/D-exchange studies of folding intermediates
    • Baldwin, R.L. Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3:84-91, 1993.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 84-91
    • Baldwin, R.L.1
  • 145
    • 0029294745 scopus 로고
    • All roads lead to Rome? The multiple pathways of protein folding
    • Weissman, J.S. All roads lead to Rome? The multiple pathways of protein folding. Curr. Biol. 2:255-260, 1995.
    • (1995) Curr. Biol. , vol.2 , pp. 255-260
    • Weissman, J.S.1
  • 146
    • 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., Nagamura, T. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 221:115-118, 1987.
    • (1987) FEBS Lett. , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 147
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Kuroda, Y, Tanaka, T., Goto, Y. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254:737-746, 1995.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 148
    • 0028978422 scopus 로고
    • Trifluoroethanolinduced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K., Goto, Y. Trifluoroethanolinduced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding. J. Mol. Biol. 245:180-194, 1995.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 149
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediates in the refolding of β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Segawa, S.-I., Goto, Y. Non-native α-helical intermediates in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat, Struct. Biol. 3:868-873, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.-I.2    Goto, Y.3
  • 150
    • 0030334664 scopus 로고    scopus 로고
    • High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy
    • Kuroda, Y., Hamada, D., Tanaka, T., Goto, Y. High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. Folding Design 1:243-251, 1996.
    • (1996) Folding Design , vol.1 , pp. 243-251
    • Kuroda, Y.1    Hamada, D.2    Tanaka, T.3    Goto, Y.4
  • 151
    • 0030582679 scopus 로고    scopus 로고
    • The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
    • Kuwajima, K., Yamaya, H., Sugai, S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264:806-822, 1996.
    • (1996) J. Mol. Biol. , vol.264 , pp. 806-822
    • Kuwajima, K.1    Yamaya, H.2    Sugai, S.3
  • 152
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki, L.S., Evans, P.A., Dobson, C.M., Radford, S.E. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 33:5212-5220, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 153
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and side chain far-uv circular dichroism during the folding of hen egg white lysozyme
    • Chaffotte, A.F., Guillou, Y., Goldberg, M.E. Kinetic resolution of peptide bond and side chain far-uv circular dichroism during the folding of hen egg white lysozyme. Biochemistry 31:9694-9702, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9694-9702
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 154
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder, H., Elöve, G.A., Englander, S.W. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335:700-704, 1988.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 155
    • 0024995943 scopus 로고
    • Detection and characterization of a folding intermediate in barnase by NMR
    • Bycroft, M., Matouschek, A., Kellis, J.T., Serrano, L., Fersht, A.R. Detection and characterization of a folding intermediate in barnase by NMR. Nature 346:488-490, 1990.
    • (1990) Nature , vol.346 , pp. 488-490
    • Bycroft, M.1    Matouschek, A.2    Kellis, J.T.3    Serrano, L.4    Fersht, A.R.5
  • 156
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso, D.O.V., Dili, K.A. Solvent denaturation and stabilization of globular proteins. Biochemistry 30:5974-5985, 1991.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.O.V.1    Dili, K.A.2
  • 157
    • 0027050824 scopus 로고
    • Modeling the effects of mutations on the denatured states of proteins
    • Shortle, D., Chan, H.S., Dill, K.A. Modeling the effects of mutations on the denatured states of proteins. Protein Sci. 1:201-215, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 201-215
    • Shortle, D.1    Chan, H.S.2    Dill, K.A.3
  • 158
    • 0027715218 scopus 로고
    • Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis
    • Iwakura, M., Jones, B.E., Falzone, C.J., Matthews, C.R. Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry 32:13566-13574, 1993.
    • (1993) Biochemistry , vol.32 , pp. 13566-13574
    • Iwakura, M.1    Jones, B.E.2    Falzone, C.J.3    Matthews, C.R.4
  • 159
    • 0029786704 scopus 로고    scopus 로고
    • Denaturants can accelerate folding rates in a class of globular proteins
    • Camacho, C.J., Thirumalai, D. Denaturants can accelerate folding rates in a class of globular proteins. Protein Sci. 5:1826-1832, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 1826-1832
    • Camacho, C.J.1    Thirumalai, D.2
  • 160
    • 0019324434 scopus 로고
    • Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B
    • McCoy, L.F., Rowe, E.S., Wong, K.P. Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B. Biochemistry 19:4738-4743, 1980.
    • (1980) Biochemistry , vol.19 , pp. 4738-4743
    • McCoy, L.F.1    Rowe, E.S.2    Wong, K.P.3
  • 161
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings, P.A., Finn, B.E., Jones, B.E., Matthews, C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model. Biochemistry 32:3783-3789, 1993.
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 162
    • 0028832610 scopus 로고
    • Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism
    • Kalnin, N.N., Kuwajima, K. Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism. Proteins Struct. Funct. Genet. 23:163-176, 1995.
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 163-176
    • Kalnin, N.N.1    Kuwajima, K.2
  • 163
    • 0019434346 scopus 로고
    • Formation of the intracham disulfide bond in the constant fragment of the immunoglobulin light chain
    • Goto, Y., Hamaguchi, K. Formation of the intracham disulfide bond in the constant fragment of the immunoglobulin light chain. J. Mol. Biol. 146:321-340, 1981.
    • (1981) J. Mol. Biol. , vol.146 , pp. 321-340
    • Goto, Y.1    Hamaguchi, K.2
  • 164
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J.S., Kim, P.S. Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253:1386-1393, 1991.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 165
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M.M., Bolen, D.W. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31:4901-4907, 1992.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 166
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao, M., Bolen, D.W. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34:3771-3781, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 167
    • 0024359551 scopus 로고
    • Thermal stabilities of globular proteins
    • Dill, K.A., Alonso, D.O.V., Hutchinson, K. Thermal stabilities of globular proteins. Biochemistry 28:5439-5449, 1989.
    • (1989) Biochemistry , vol.28 , pp. 5439-5449
    • Dill, K.A.1    Alonso, D.O.V.2    Hutchinson, K.3
  • 168
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G
    • Alexander, P., Orban, J., Bryan, P. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. Biochemistry 31:7243-7248, 1992.
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 169
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley, M.L., Baker, D. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc. Natl. Acad. Sci. USA. 94:10636-10640, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 170
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R.L. On-pathway versus off-pathway folding intermediates. Folding Design 1:R1-R8, 1996.
    • (1996) Folding Design , vol.1
    • Baldwin, R.L.1
  • 171
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., Kellis, J.T., Jr., Serrano, L., Bycroft, M., Fersht, A.R. Transient folding intermediates characterized by protein engineering. Nature 346:440-445, 1990.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 172
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I.D., Roder, H. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat. Struct. Biol. 3:193-205, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 173
    • 0026975884 scopus 로고
    • Kinetic evidence of microscopic states in protein folding
    • Chen, H.M., Markin, V.S., Tsong, T.Y. Kinetic evidence of microscopic states in protein folding. Biochemistry 31: 12369-12375, 1992.
    • (1992) Biochemistry , vol.31 , pp. 12369-12375
    • Chen, H.M.1    Markin, V.S.2    Tsong, T.Y.3
  • 177
    • 0000346442 scopus 로고
    • The application of the theory of absolute reaction rates to proteins
    • Eyring, H., Stearn, A.E. The application of the theory of absolute reaction rates to proteins. Chem. Rev. 24:253-270, 1939.
    • (1939) Chem. Rev. , vol.24 , pp. 253-270
    • Eyring, H.1    Stearn, A.E.2
  • 178
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., 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. 224:771-782, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 179
    • 0026579572 scopus 로고
    • The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
    • Serrano, L., Matouschek, A., Fersht, A.R. The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224:805-818, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 180
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • Jackson, S.E., eIMasry, N., Fersht, A.R. Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis. Biochemistry 32:11270-11278, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    EIMasry, N.2    Fersht, A.R.3
  • 181
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A.R. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA 92:10869-10873, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 184
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S.J., Hofrichter, J., Szabo, A., Eaton, W.A. Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA 93:11615-11617, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 185
    • 0018197424 scopus 로고
    • Mechanisms of the multiphasic kinetics in the folding and unfolding of globular proteins
    • Kanehisa, M.I., Tsong, T.Y. Mechanisms of the multiphasic kinetics in the folding and unfolding of globular proteins. J. Mol. Biol. 124:177-194, 1978.
    • (1978) J. Mol. Biol. , vol.124 , pp. 177-194
    • Kanehisa, M.I.1    Tsong, T.Y.2
  • 186
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • Doyle, R., Simons, K., Qian, H., Baker, D. Local interactions and the optimization of protein folding. Proteins 29:282-291, 1997.
    • (1997) Proteins , vol.29 , pp. 282-291
    • Doyle, R.1    Simons, K.2    Qian, H.3    Baker, D.4
  • 187
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model
    • Mirny, L.A., Abkevich, V., Shakhnovich, E.I. Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model. Folding Design 1:103-116, 1996.
    • (1996) Folding Design , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 189
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C.M., Henry, E.R., Hofrichter, J., Eaton, W.A. The role of solvent viscosity in the dynamics of protein conformational changes. Science 256:1796-1798, 1992.
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 190
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger, C.D., Jonsson, T., Sauer, R.T. Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. USA 93:2629-2634, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 191
    • 0029866436 scopus 로고    scopus 로고
    • Why is protein folding so fast?
    • Baldwin, R.L. Why is protein folding so fast? Proc. Natl. Acad. Sci. USA 93:2627-2628, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2627-2628
    • Baldwin, R.L.1
  • 192
    • 0000399469 scopus 로고    scopus 로고
    • Viscosity dependence of the folding rates of proteins
    • Klimov, D.K., Thirumalai, D. Viscosity dependence of the folding rates of proteins. Phys. Rev. Lett. 79:317-320, 1997.
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 317-320
    • Klimov, D.K.1    Thirumalai, D.2
  • 193
    • 6844267353 scopus 로고
    • Reply to "Kinetics of protein folding"
    • Karplus, M., Šali, A., Shakhnovich, E. Reply to "Kinetics of protein folding." Nature 373:665, 1995.
    • (1995) Nature , vol.373 , pp. 665
    • Karplus, M.1    Šali, A.2    Shakhnovich, E.3
  • 194
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich, E.I. Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7:29-40, 1997.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 196
    • 0030626588 scopus 로고    scopus 로고
    • The Levinthal paradox: Yesterday and today
    • Karplus, M. The Levinthal paradox: yesterday and today. Folding & Design 2:S69-S75, 1997.
    • (1997) Folding & Design , vol.2
    • Karplus, M.1
  • 197
    • 6844238811 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • In Press
    • Dobson, C.M. Šali, A., Karplus, M. Protein folding: A perspective from theory and experiment. Angewandte Chemie. In Press.
    • Angewandte Chemie
    • Dobson, C.M.1    Šali, A.2    Karplus, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.