메뉴 건너뛰기




Volumn 115, Issue 2-3 SPEC. ISS., 2005, Pages 169-175

Native geometry and the dynamics of protein folding

Author keywords

Contact order; Cooperativity; Kinetics; Lattice models; Long range contacts; Protein folding

Indexed keywords

AMINO ACID;

EID: 14744273112     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.12.022     Document Type: Conference Paper
Times cited : (14)

References (27)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small protein molecules fold?
    • S.E. Jackson How do small protein molecules fold? Fold. Des. 3 1998 81 91
    • (1998) Fold. Des. , vol.3 , pp. 81-91
    • Jackson, S.E.1
  • 2
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • K.W. Plaxco, K.T. Simmons, and D. Baker 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    Simmons, K.T.2    Baker, D.3
  • 3
    • 0042130544 scopus 로고    scopus 로고
    • Simple two-state protein folding kinetics requires near-levinthal thermodynamic cooperativity
    • H. Kaya, and H.S. Chan Simple two-state protein folding kinetics requires near-levinthal thermodynamic cooperativity Proteins 52 2003 510 523
    • (2003) Proteins , vol.52 , pp. 510-523
    • Kaya, H.1    Chan, H.S.2
  • 4
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • J.D. Bryngelson, and P.G. Wolynes Spin glasses and the statistical mechanics of protein folding Proc. Natl. Acad. Sci. U. S. A. 84 1987 7524 7528
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 5
    • 0026723063 scopus 로고
    • Protein folding funnels-a kinetic approach to the sequence structure relationship
    • P.E. Leopold, M. Montal, and J.N. Onuchic Protein folding funnels-a kinetic approach to the sequence structure relationship Proc. Natl. Acad. Sci. U. S. A. 89 1992 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
  • 6
    • 0032978994 scopus 로고    scopus 로고
    • Polypeptide chain collapse can occur concomitantly with the rate limiting step in protein folding
    • K.W. Plaxco, I.S. Millet, D.J. Segel, S. Doniach, and D. Baker Polypeptide chain collapse can occur concomitantly with the rate limiting step in protein folding Nat. Struct. Biol. 6 1999 554 557
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 554-557
    • Plaxco, K.W.1    Millet, I.S.2    Segel, D.J.3    Doniach, S.4    Baker, D.5
  • 7
    • 0034710944 scopus 로고    scopus 로고
    • Non-glassy kinetics in the folding of a simple single domain protein
    • B. Gillespie, and K.W. Plaxco Non-glassy kinetics in the folding of a simple single domain protein Proc. Natl. Acad. Sci. U. S. A. 97 2000 12014 12019
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12014-12019
    • Gillespie, B.1    Plaxco, K.W.2
  • 8
    • 0033535839 scopus 로고    scopus 로고
    • Cytochrome b(562) folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein
    • P. Wittung-Stafshede, J.C. Lee, J.R. Winkler, and H.B. Gray Cytochrome b(562) folding triggered by electron transfer: approaching the speed limit for formation of a four-helix-bundle protein Proc. Natl. Acad. Sci. U. S. A. 96 1999 6587 6590
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6587-6590
    • Wittung-Stafshede, P.1    Lee, J.C.2    Winkler, J.R.3    Gray, H.B.4
  • 10
    • 0034687123 scopus 로고    scopus 로고
    • Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
    • K.W. Plaxco, K.T. Simmons, I. Ruczinski, and D. Baker Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics Biochemistry 39 2000 11177 11183
    • (2000) Biochemistry , vol.39 , pp. 11177-11183
    • Plaxco, K.W.1    Simmons, K.T.2    Ruczinski, I.3    Baker, D.4
  • 11
    • 0000355428 scopus 로고
    • Respective role of short- and long-range interactions in protein folding
    • N. Gō, and H. Taketomi Respective role of short- and long-range interactions in protein folding Proc. Natl. Acad. Sci. U. S. A. 75 1978 559 563
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 559-563
    • Go, N.1    Taketomi, H.2
  • 12
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • V.I. Abkevich, A.M. Gutin, and E.I. Shakhnovich 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
  • 13
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • R. Doyle, K. Simmons, H. Qian, and D. Baker Local interactions and the optimization of protein folding Proteins 29 1997 282 291
    • (1997) Proteins , vol.29 , pp. 282-291
    • Doyle, R.1    Simmons, K.2    Qian, H.3    Baker, D.4
  • 14
    • 0032979568 scopus 로고    scopus 로고
    • Importance of long-range interactions in protein folding
    • M.M. Gromiha, and S. Selvaraj Importance of long-range interactions in protein folding Biophys. Chem. 77 1999 49 68
    • (1999) Biophys. Chem. , vol.77 , pp. 49-68
    • Gromiha, M.M.1    Selvaraj, S.2
  • 15
    • 0015597839 scopus 로고
    • Nucleation, rapid folding, and globular intrachain regions in proteins
    • D.B. Wetlaufer Nucleation, rapid folding, and globular intrachain regions in proteins Proc. Natl. Acad. Sci. U. S. A. 70 1973 697 701
    • (1973) Proc. Natl. Acad. Sci. U. S. A. , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 16
    • 0030604696 scopus 로고    scopus 로고
    • Local Interactions dominate folding in a simple lattice protein model
    • R. Unger, and J. Moult Local Interactions dominate folding in a simple lattice protein model J. Mol. Biol. 259 1996 988 994
    • (1996) J. Mol. Biol. , vol.259 , pp. 988-994
    • Unger, R.1    Moult, J.2
  • 17
    • 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 prediction
    • M.M. Gromiha, and S. Selvaraj Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding prediction J. Mol. Biol. 310 2001 27 32
    • (2001) J. Mol. Biol. , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 18
    • 14744273094 scopus 로고    scopus 로고
    • Proceedings of the International School of Physics Enrico Fermi, Course CXLV
    • R.A. Broglia E.I. Shakhnovich IOS Press Ohmusha
    • L. Mirny, and E.I. Shakhnovich R.A. Broglia E.I. Shakhnovich Proceedings of the International School of Physics Enrico Fermi, Course CXLV Protein Folding Evolution Design 2001 IOS Press Ohmusha 38
    • (2001) Protein Folding Evolution Design , pp. 38
    • Mirny, L.1    Shakhnovich, E.I.2
  • 19
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal-structures-quasi-chemical approximation
    • S. Miyazawa, and R.L. Jernigan Estimation of effective interresidue contact energies from protein crystal-structures-quasi-chemical approximation Macromolecules 18 1985 534 552
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 22
    • 0027234766 scopus 로고
    • Engineering of stable and fast-folding sequences of model proteins
    • E.I. Shakhnovich, and A.M. Gutin Engineering of stable and fast-folding sequences of model proteins Proc. Natl. Acad. Sci. U. S. A. 90 1993 7195 7199
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7195-7199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 23
    • 0037156117 scopus 로고    scopus 로고
    • Thermodynamic control and dynamical regimes in protein folding
    • P.F.N. Faisca, and R.C. Ball Thermodynamic control and dynamical regimes in protein folding J. Chem. Phys. 116 2002 7231 7238
    • (2002) J. Chem. Phys. , vol.116 , pp. 7231-7238
    • Faisca, P.F.N.1    Ball, R.C.2
  • 24
    • 0037044965 scopus 로고    scopus 로고
    • Topological complexity, contact order and protein folding rates
    • P.F.N. Faisca, and R.C. Ball 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
  • 25
    • 0037423710 scopus 로고    scopus 로고
    • Cooperativity, smooth energy landscapes and the origins of topology-dependent kinetics protein folding rates
    • A.I. Jewett, V.S. Pande, and K.W. Plaxco Cooperativity, smooth energy landscapes and the origins of topology-dependent kinetics protein folding rates J. Mol. Biol. 326 2003 247 253
    • (2003) J. Mol. Biol. , vol.326 , pp. 247-253
    • Jewett, A.I.1    Pande, V.S.2    Plaxco, K.W.3
  • 26
    • 0042631521 scopus 로고    scopus 로고
    • Contact order dependent protein folding rates: Kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences
    • H. Kaya, and H.S. Chan Contact order dependent protein folding rates: kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences Proteins 52 2003 524 533
    • (2003) Proteins , vol.52 , pp. 524-533
    • Kaya, H.1    Chan, H.S.2
  • 27
    • 42749107023 scopus 로고    scopus 로고
    • Folding and form: Insights from lattice simulations
    • P.F.N. Faisca, M.M. Telo da Gama, and R.C. Ball Folding and form: insights from lattice simulations Phys. Rev. E 69 2004 51917
    • (2004) Phys. Rev. e , vol.69 , pp. 51917
    • Faisca, P.F.N.1    Telo Da Gama, M.M.2    Ball, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.