메뉴 건너뛰기




Volumn 31, Issue 8, 1998, Pages 433-440

Theory of Two-State Cooperative Folding of Proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0001109173     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar960288q     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō, N. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 1983, 12, 183-210.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 2
    • 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. U.S.A. 1987, 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 3
    • 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. U.S.A. 1992, 89, 8721-8725.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 5
    • 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. 1997, 4, 10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 6
    • 0028270634 scopus 로고
    • Kinetics of protein folding. A lattice model study of the requirements for folding to the native state
    • Sali, A.; Shakhnovich, E. I.; Karplus, M. Kinetics of protein folding. A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 1994, 235, 1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.I.2    Karplus, M.3
  • 7
    • 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. 1997, 7, 29-40.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 8
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D.; Onuchic, J. N.; Socci, N. D.; Wolynes, P. G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 1995, 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 10
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • Privalov, P. L. Stability of proteins. Small globular proteins. Adv. Protein Chem. 1979, 33, 167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 11
    • 0020348367 scopus 로고
    • Stability of proteins which do not present a single cooperative system
    • Privalov, P. L. Stability of 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
  • 12
    • 84984082911 scopus 로고
    • Statistical mechanics of noncovalent bonds in polyamino acids. IX. The two-state theory of protein denaturation
    • Poland, D. C.; Scheraga, H. A. Statistical mechanics of noncovalent bonds in polyamino acids. IX. The two-state theory of protein denaturation. Biopolymers 1965, 3, 401-419.
    • (1965) Biopolymers , vol.3 , pp. 401-419
    • Poland, D.C.1    Scheraga, H.A.2
  • 13
    • 0016812958 scopus 로고
    • Theory of reversible denaturation of globular proteins
    • Gō, N. Theory of reversible denaturation of globular proteins. Int. J. Pept. Protein Res. 1975, 7, 313-323.
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 313-323
    • Go, N.1
  • 14
    • 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. 1994, 98, 4940-4948.
    • (1994) J. Phys. Chem. , vol.98 , pp. 4940-4948
    • Hao, M.-H.1    Scheraga, H.A.2
  • 15
    • 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. 1994, 98, 9882-9893.
    • (1994) J. Phys. Chem. , vol.98 , pp. 9882-9893
    • Hao, M.-H.1    Scheraga, H.A.2
  • 16
    • 0000091698 scopus 로고
    • First-order phase transitions in the canonical and the microcanonical ensemble
    • Huiler, A. First-order phase transitions in the canonical and the microcanonical ensemble. Z. Phys. B 1994, 93, 401-405.
    • (1994) Z. Phys. B , vol.93 , pp. 401-405
    • Huiler, A.1
  • 17
    • 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. 1996, 104, 5860-5868.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 18
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M.; Swendsen, R. H. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 1989, 63, 1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 19
    • 0001629677 scopus 로고
    • New approach to spin-glass simulations
    • Berg, B. A.; Celik, T. New approach to spin-glass simulations. Phys. Rev. Lett. 1992, 69, 2292-2295.
    • (1992) Phys. Rev. Lett. , vol.69 , pp. 2292-2295
    • Berg, B.A.1    Celik, T.2
  • 20
    • 0002061484 scopus 로고
    • New Monte Carlo algorithm: Entropy sampling
    • Erratum, 1993, 71, 2353
    • Lee, J. New Monte Carlo algorithm: entropy sampling. Phys. Rev. Lett. 1993, 71, 211-214; Erratum, 1993, 71, 2353.
    • (1993) Phys. Rev. Lett. , vol.71 , pp. 211-214
    • Lee, J.1
  • 21
    • 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. U.S.A. 1996, 93, 4984-4989.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4984-4989
    • Hao, M.-H.1    Scheraga, H.A.2
  • 22
    • 0000829596 scopus 로고    scopus 로고
    • Optimizing potential functions for protein folding
    • Hao, M.-H.; Scheraga, H. A. Optimizing potential functions for protein folding. J. Phys. Chem. 1996, 700, 14540-14548.
    • (1996) J. Phys. Chem. , vol.100 , pp. 14540-14548
    • Hao, M.-H.1    Scheraga, H.A.2
  • 23
    • 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. 1991, 20, 447-490.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 447-490
    • Chan, H.S.1    Dill, K.A.2
  • 24
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Shakhnovich, E. I. Proteins with selected sequences fold into unique native conformation. Phys. Rev. Lett. 1994, 72, 3907-3910.
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 26
    • 0029155772 scopus 로고
    • Impact of local and nonlocal interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V. I.; Gutin, A. M.; Shakhnovich, E. I. Impact of local and nonlocal interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 1995, 252, 460-471.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 27
    • 0001842441 scopus 로고    scopus 로고
    • Adding backbone to protein folding: Why proteins are polypeptides
    • Honig, B.; Cohen, F. E. Adding backbone to protein folding: why proteins are polypeptides. Folding Design, 1996, 1, R17-R20.
    • (1996) Folding Design , vol.1
    • Honig, B.1    Cohen, F.E.2
  • 28
    • 0025608908 scopus 로고
    • Simulations of the folding of a globular protein
    • Skolnick, J.; Kolinski, A. Simulations of the folding of a globular protein. Science 1990, 250, 1121-1125.
    • (1990) Science , vol.250 , pp. 1121-1125
    • Skolnick, J.1    Kolinski, A.2
  • 29
    • 0000778903 scopus 로고
    • A general method for the prediction of the three-dimensional structure and folding pathway of globular proteins: Application to designed helical proteins
    • Kolinski, A.; Godzik, A.; Skolnick, J. A general method for the prediction of the three-dimensional structure and folding pathway of globular proteins: application to designed helical proteins. J. Chem. Phys. 1993, 98, 7420-7433.
    • (1993) J. Chem. Phys. , vol.98 , pp. 7420-7433
    • Kolinski, A.1    Godzik, A.2    Skolnick, J.3
  • 30
    • 0000671822 scopus 로고
    • Computer design of idealized β- Motifs
    • Kolinski, A.; Galazka, W.; Skolnick, J. Computer design of idealized β-motifs. J. Chem. Phys. 1995, 103, 10286-10297.
    • (1995) J. Chem. Phys. , vol.103 , pp. 10286-10297
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 31
    • 0029809182 scopus 로고    scopus 로고
    • On the origin of the cooperativity of protein folding - Implications from model simulations
    • Kolinski, A.; Galazka, W.; Skolnick, J. On the origin of the cooperativity of protein folding - Implications from model simulations. Proteins 1996, 26, 271-287.
    • (1996) Proteins , vol.26 , pp. 271-287
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 32
    • 11744314103 scopus 로고
    • Statistical thermodynamics of protein folding: Comparison of a mean-field theory with Monte Carlo simulation
    • Hao, M.-H.; Scheraga, H. A. Statistical thermodynamics of protein folding: comparison of a mean-field theory with Monte Carlo simulation. J. Chem. Phys. 1995, 102, 1334-1348.
    • (1995) J. Chem. Phys. , vol.102 , pp. 1334-1348
    • Hao, M.-H.1    Scheraga, H.A.2
  • 33
    • 0031259239 scopus 로고    scopus 로고
    • On foldable protein-like models; a statistical-mechanical study with Monte Carlo simulations
    • Hao, M.-H.; Scheraga, H. A. On foldable protein-like models; a statistical-mechanical study with Monte Carlo simulations. Physica A 1997, 244, 124-146.
    • (1997) Physica A , vol.244 , pp. 124-146
    • Hao, M.-H.1    Scheraga, H.A.2
  • 34
    • 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. U.S.A. 1993, 90, 6369-6372.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 35
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free-energy of a three-helix bundle protein
    • Boczko, E. M.; Brooks, C. L. First-principles calculation of the folding free-energy of a three-helix bundle protein. Science 1995, 269, 393-396.
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks, C.L.2
  • 36
    • 85033904608 scopus 로고    scopus 로고
    • Molecular mechanisms for cooperative folding of proteins
    • in press
    • Hao, M.-H.; Scheraga, H. A. Molecular mechanisms for cooperative folding of proteins. J. Mol. Biol., in press.
    • J. Mol. Biol.
    • Hao, M.-H.1    Scheraga, H.A.2
  • 37
    • 0012275844 scopus 로고    scopus 로고
    • Characterization of foldable protein models: Thermodynamics, folding kinetics, and force field
    • Hao, M.-H.; Scheraga, H. A. Characterization of foldable protein models: thermodynamics, folding kinetics, and force field. J. Chem. Phys. 1997, 107, 8089-8102.
    • (1997) J. Chem. Phys. , vol.107 , pp. 8089-8102
    • Hao, M.-H.1    Scheraga, H.A.2
  • 38
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • Zwanzig, Z. Simple model of protein folding kinetics. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 9801-9804.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9801-9804
    • Zwanzig, Z.1
  • 39
    • 0027234766 scopus 로고
    • Engineering of stable and fast-folding sequences of model proteins
    • Shakhnovich, E. L; Gutin, A. M. Engineering of stable and fast-folding sequences of model proteins. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 7195-7199.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7195-7199
    • Shakhnovich, E.L.1    Gutin, A.M.2
  • 40
    • 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. 1990, 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 42
    • 0030596063 scopus 로고    scopus 로고
    • How to derive a protein folding potential? A new approach to an old problem
    • Mirny, L. A.; Shakhnovich, E. I. How to derive a protein folding potential? A new approach to an old problem. J. Mol. Biol. 1996, 264, 1164-1179.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1164-1179
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 43
    • 4243719017 scopus 로고    scopus 로고
    • New algorithm for protein design
    • Deutsch, J. M.; Kurosky, T. New algorithm for protein design. Phys. Rev. Lett. 1996, 76, 323-326.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 323-326
    • Deutsch, J.M.1    Kurosky, T.2
  • 44
    • 0029909384 scopus 로고    scopus 로고
    • An iterative method for extracting energy-like quantities from protein structures
    • Thomas, P. D.; Dill, K. A. An iterative method for extracting energy-like quantities from protein structures. Proc. Natl.Acad. Sci. U.S.A. 1996, 93, 11628-11633.
    • (1996) Proc. Natl.Acad. Sci. U.S.A. , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.