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Volumn 326, Issue 1, 2003, Pages 247-253

Cooperativity, smooth energy landscapes and the origins of topology-dependent protein folding rates

Author keywords

Contact order; Non additivity; Topological frustration

Indexed keywords

POLYMER; PROTEIN;

EID: 0037423710     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01356-6     Document Type: Article
Times cited : (80)

References (32)
  • 1
    • 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. 93:1989;6902-6915.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 3
    • 4243572706 scopus 로고    scopus 로고
    • Criterion that determines the foldability of proteins
    • Klimov D.K., Thirumalai D. Criterion that determines the foldability of proteins. Phys. Rev. Lett. 76:1996;4070-4073.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 4070-4073
    • Klimov, D.K.1    Thirumalai, D.2
  • 4
    • 0028270634 scopus 로고
    • Kinetics of protein-folding: A lattice model study of the requirements for folding to the native state
    • Sali 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. 235:1994;1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 5
    • 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. 252:1995;460-471.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 7
    • 0034710944 scopus 로고    scopus 로고
    • Non-glassy kinetics in the folding of a simple, single domain protein
    • Gillespie B., Plaxco K.W. Non-glassy kinetics in the folding of a simple, single domain protein. Proc. Natl Acad. Sci. USA. 97:2000;12014-12019.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12014-12019
    • Gillespie, B.1    Plaxco, K.W.2
  • 9
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 10
    • 0034687123 scopus 로고    scopus 로고
    • Sequence, stability, topology and length; The determinants of two-state protein folding kinetics
    • Plaxco K.W., Simons K.T., Ruczinski I., Baker D. Sequence, stability, topology and length; the determinants of two-state protein folding kinetics. Biochemistry. 39:2000;11177-11183.
    • (2000) Biochemistry , vol.39 , pp. 11177-11183
    • Plaxco, K.W.1    Simons, K.T.2    Ruczinski, I.3    Baker, D.4
  • 11
    • 0035967862 scopus 로고    scopus 로고
    • Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction
    • Gromiha M.M., Selvaraj S. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction. J. Mol. Biol. 310:2001;27-32.
    • (2001) J. Mol. Biol. , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 12
    • 0036215854 scopus 로고    scopus 로고
    • Folding rate prediction using total contact distance
    • Zhou H.Y., Zhou Y.Q. Folding rate prediction using total contact distance. Biophys. J. 82:2002;458-463.
    • (2002) Biophys. J. , vol.82 , pp. 458-463
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 13
    • 0013498088 scopus 로고    scopus 로고
    • The topomer search model; A quantitative, first principles description of two-state protein folding kinetics
    • In press
    • Makarov D.E., Plaxco K.W. The topomer search model; a quantitative, first principles description of two-state protein folding kinetics. Protein Sci. 2002;. In press.
    • (2002) Protein Sci.
    • Makarov, D.E.1    Plaxco, K.W.2
  • 14
    • 3943055270 scopus 로고
    • Noninteracting local-structure model of folding and unfolding transition in globular proteins. II. Application to two-dimensional lattice proteins
    • Abe H., Go N. Noninteracting local-structure model of folding and unfolding transition in globular proteins. II. Application to two-dimensional lattice proteins. Biopolymers. 20:1981;10113-11031.
    • (1981) Biopolymers , vol.20 , pp. 10113-11031
    • Abe, H.1    Go, N.2
  • 15
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Gō-like model
    • Koga N., Takada S. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Gō-like model. J. Mol. Biol. 313:2001;171-180.
    • (2001) J. Mol. Biol. , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 16
    • 0013463122 scopus 로고    scopus 로고
    • Universality classes in folding times of proteins
    • In press
    • Cieplak M., Hoang T.X. Universality classes in folding times of proteins. Biophys. J. 2002;. In press.
    • (2002) Biophys. J.
    • Cieplak, M.1    Hoang, T.X.2
  • 17
    • 0035826032 scopus 로고    scopus 로고
    • Role of explicitly cooperative interactions in protein folding funnels: A simulation study
    • Eastwood M.P., Wolynes P.G. Role of explicitly cooperative interactions in protein folding funnels: a simulation study. J. Chem. Phys. 114:2001;4702-4716.
    • (2001) J. Chem. Phys. , vol.114 , pp. 4702-4716
    • Eastwood, M.P.1    Wolynes, P.G.2
  • 19
    • 0031576341 scopus 로고    scopus 로고
    • Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2
    • Ladurner A.G., Itzhaki L.S., Gay G.D., Fersht A.R. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2. J. Mol. Biol. 273:1997;317-329.
    • (1997) J. Mol. Biol. , vol.273 , pp. 317-329
    • Ladurner, A.G.1    Itzhaki, L.S.2    Gay, G.D.3    Fersht, A.R.4
  • 21
    • 0033607208 scopus 로고    scopus 로고
    • Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of protein A
    • Shea J.E., Onuchic J.N., Brooks C.L. Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A. Proc. Natl Acad. Sci. USA. 96:1999;12512-12517.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12512-12517
    • Shea, J.E.1    Onuchic, J.N.2    Brooks, C.L.3
  • 23
    • 0007463680 scopus 로고    scopus 로고
    • Statistical mechanics of a correlated energy landscape model for protein folding funnels
    • Plotkin S.S., Wang J., Wolynes P.G. Statistical mechanics of a correlated energy landscape model for protein folding funnels. J. Chem. Phys. 106:1997;2932-2948.
    • (1997) J. Chem. Phys. , vol.106 , pp. 2932-2948
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 25
    • 0036643497 scopus 로고    scopus 로고
    • Anti-cooperativity and cooperativity in hydrophobic interactions: Three-body free energy landscapes and comparison with implicit-solvent potential functions for proteins
    • Shimizu S., Chan H.S. Anti-cooperativity and cooperativity in hydrophobic interactions: three-body free energy landscapes and comparison with implicit-solvent potential functions for proteins. Proteins: Struct. Funct. Genet. 48:2002;15-30.
    • (2002) Proteins: Struct. Funct. Genet. , vol.48 , pp. 15-30
    • Shimizu, S.1    Chan, H.S.2
  • 26
    • 0036304480 scopus 로고    scopus 로고
    • Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: How applicable is the transition state picture to folding and unfolding?
    • Kaya H., Chan H.S. Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: how applicable is the transition state picture to folding and unfolding? J. Mol. Biol. 315:2002;899-909.
    • (2002) J. Mol. Biol. , vol.315 , pp. 899-909
    • Kaya, H.1    Chan, H.S.2
  • 27
    • 0037091023 scopus 로고    scopus 로고
    • Three-body correlations in protein folding: The origin of cooperativity
    • Fernandez A., Colubri A., Berry R.S. Three-body correlations in protein folding: the origin of cooperativity. Physica A. 307:2002;235-259.
    • (2002) Physica A , vol.307 , pp. 235-259
    • Fernandez, A.1    Colubri, A.2    Berry, R.S.3
  • 28
    • 0035813361 scopus 로고    scopus 로고
    • Protein folding cooperativity in the correlated lattice
    • Fernandez A. Protein folding cooperativity in the correlated lattice. Phys. Lett. A. 290:2001;101-105.
    • (2001) Phys. Lett. A , vol.290 , pp. 101-105
    • Fernandez, A.1
  • 29
    • 36449008575 scopus 로고
    • Energy landscapes and the collapse dynamics of homopolymers
    • Chan H.S., Dill K.A. Energy landscapes and the collapse dynamics of homopolymers. J. Chem. Phys. 99:1993;2116-2127.
    • (1993) J. Chem. Phys. , vol.99 , pp. 2116-2127
    • Chan, H.S.1    Dill, K.A.2
  • 30
    • 33846096753 scopus 로고
    • Monte Carlo calculations on dynamics of polymers in dilute solution
    • Verdier P.H., Stockmayer W.H. Monte Carlo calculations on dynamics of polymers in dilute solution. J. Chem. Phys. 36:1962;227-235.
    • (1962) J. Chem. Phys. , vol.36 , pp. 227-235
    • Verdier, P.H.1    Stockmayer, W.H.2
  • 31
    • 34250103739 scopus 로고
    • Nonergodicity of local, length-conserving Monte-Carlo algorithms for the self-avoiding walk
    • Madras N., Sokal A.D. Nonergodicity of local, length-conserving Monte-Carlo algorithms for the self-avoiding walk. J. Stat. Phys. 47:1987;573-595.
    • (1987) J. Stat. Phys. , vol.47 , pp. 573-595
    • Madras, N.1    Sokal, A.D.2
  • 32
    • 0037044965 scopus 로고    scopus 로고
    • Topological complexity, contact order, and protein folding rates
    • Faisca P.F.N., Ball R.C. Topological complexity, contact order, and protein folding rates. J. Chem. Phys. 117:2002;8587-8591.
    • (2002) J. Chem. Phys. , vol.117 , pp. 8587-8591
    • Faisca, P.F.N.1    Ball, R.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.