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Volumn 6, Issue 2, 1997, Pages 347-354

A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding

Author keywords

hydrophobic interaction; potential of mean force; protein folding

Indexed keywords

ARTICLE; CHEMICAL REACTION KINETICS; COMPUTER SIMULATION; DIMERIZATION; HYDROPHOBICITY; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN FOLDING; SOLVATION;

EID: 0031052147     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060210     Document Type: Article
Times cited : (106)

References (32)
  • 4
    • 0029151245 scopus 로고
    • First principles calculation of the folding free energy of a three-helix bundle protein
    • Brooks CL, Boczko EM. 1995. First principles calculation of the folding free energy of a three-helix bundle protein. Science 269:393-396.
    • (1995) Science , vol.269 , pp. 393-396
    • Brooks, C.L.1    Boczko, E.M.2
  • 5
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly ML. 1983. Analytical molecular surface calculation. J Appl Crystallogr 16:548-558.
    • (1983) J Appl Crystallogr , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 6
    • 0027219504 scopus 로고
    • Protein unfolding pathways explored through molecular dynamics simulations
    • Daggett V, Levitt M. 1993. Protein unfolding pathways explored through molecular dynamics simulations. J Mol Biol 232:600-619.
    • (1993) J Mol Biol , vol.232 , pp. 600-619
    • Daggett, V.1    Levitt, M.2
  • 7
    • 0028231194 scopus 로고
    • Protein folding ↔ unfolding dynamics
    • Daggett V, Levitt M. 1994. Protein folding ↔ unfolding dynamics. Curr Opin Struct Biol 4:291-295.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 291-295
    • Daggett, V.1    Levitt, M.2
  • 8
    • 0343368213 scopus 로고
    • The stabilities of globular proteins
    • Oxender DL, Fox CF, eds.
    • Dill K 1987. The stabilities of globular proteins. In: Oxender DL, Fox CF, eds. Protein engineering. pp 187-192.
    • (1987) Protein Engineering , pp. 187-192
    • Dill, K.1
  • 9
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.1
  • 10
    • 0003742069 scopus 로고
    • London: University College, Department of Biochemistry and Molecular Biology
    • Hubbard SJ, Thornton JM. 1993. NACCESS computer program. London: University College, Department of Biochemistry and Molecular Biology.
    • (1993) NACCESS Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 11
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki LS, Otzen DE, Fersht AR. 1995. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 254:260-288.
    • (1995) J Mol Biol , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 12
    • 0028180523 scopus 로고
    • Application of scaled particle theory to model the hydrophobic effect: Implications for molecular association and protein stability
    • Jackson RM, Sternberg MJ. 1994. Application of scaled particle theory to model the hydrophobic effect: Implications for molecular association and protein stability. Protein Eng 7:371-384.
    • (1994) Protein Eng , vol.7 , pp. 371-384
    • Jackson, R.M.1    Sternberg, M.J.2
  • 13
  • 14
    • 36549092795 scopus 로고
    • Efficient computation of absolute free energies of binding by computer simulations. Application to the methane dimer in water
    • Jorgenson WL, Buckner JK, Boudon S, Tirado-Rives J. 1988. Efficient computation of absolute free energies of binding by computer simulations. Application to the methane dimer in water. J Chem Phys 89:3742.
    • (1988) J Chem Phys , vol.89 , pp. 3742
    • Jorgenson, W.L.1    Buckner, J.K.2    Boudon, S.3    Tirado-Rives, J.4
  • 16
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus M, Sali A. 1995. Theoretical studies of protein folding and unfolding. Curr Opin Struct Biol 5:58-73.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 17
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 18
    • 0028931751 scopus 로고
    • Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange
    • Kiefhaber T, Baldwin RL. 1995. Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. Proc Natl Acad Sci USA 92:2657-2661.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2657-2661
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 19
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
    • Li A, Daggett V. 1994. Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2. Proc Natl Acad Sci USA 91:10430-10434.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 20
    • 0026588145 scopus 로고
    • Theory of hydrophobicity: Transient cavities in molecular liquids
    • Pratt LR, Pohorille A. 1992. Theory of hydrophobicity: Transient cavities in molecular liquids. Proc Natl Acad Sci USA 89:2995-2999.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2995-2999
    • Pratt, L.R.1    Pohorille, A.2
  • 21
    • 0002278843 scopus 로고
    • Scaled particle methods in the statistical thermodynamics of fluids
    • Reiss H. 1965. Scaled particle methods in the statistical thermodynamics of fluids. Adv Chem Phys 9:1-84.
    • (1965) Adv Chem Phys , vol.9 , pp. 1-84
    • Reiss, H.1
  • 22
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM. 1977. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng 6:151-176.
    • (1977) Annu Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 23
    • 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 AR. 1992. 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) J Mol Biol , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 24
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl MJ. 1995. Knowledge-based potentials for proteins. Curr Opin Struct Biol 5:229-235.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 25
    • 36448999843 scopus 로고
    • Free energy, entropy, and internal energy of hydrophobic interactions: Computer simulations
    • Smith DE, Haymet ADJ. 1993. Free energy, entropy, and internal energy of hydrophobic interactions: Computer simulations. J Chem Phys 98:6445-54.
    • (1993) J Chem Phys , vol.98 , pp. 6445-6454
    • Smith, D.E.1    Haymet, A.D.J.2
  • 26
    • 0027092952 scopus 로고
    • Molecular surface area and the hydrophobic effect
    • Tunon I, Silla E, Pascual-Ahuir JL. 1992. Molecular surface area and the hydrophobic effect. Protein Eng 5:715-716.
    • (1992) Protein Eng , vol.5 , pp. 715-716
    • Tunon, I.1    Silla, E.2    Pascual-Ahuir, J.L.3
  • 27
    • 0028905560 scopus 로고
    • Evidence for a molten globule-like state in protein folding from determination of activation volumes
    • Vidugiris GJA, Markley JL, Royer CA. 1995. Evidence for a molten globule-like state in protein folding from determination of activation volumes. Biochemistry 34:4909-4912.
    • (1995) Biochemistry , vol.34 , pp. 4909-4912
    • Vidugiris, G.J.A.1    Markley, J.L.2    Royer, C.A.3
  • 28
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger CD, Jonsson T, Sauer RT 1996. 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) Proc Natl Acad Sci USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 29
    • 33751499566 scopus 로고
    • Molecular dynamics study of a hydrophobic aggregate in an aqueous solution of methane
    • Wallqvist A. 1991. Molecular dynamics study of a hydrophobic aggregate in an aqueous solution of methane. J Phys Chem 95:8921-8927.
    • (1991) J Phys Chem , vol.95 , pp. 8921-8927
    • Wallqvist, A.1
  • 31
    • 0025017318 scopus 로고
    • Differences between pair and bulk hydrophobic interactions
    • Wood RH, Thompson PT. 1990. Differences between pair and bulk hydrophobic interactions. Proc Natl Acad Sci USA 87:946-949.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 946-949
    • Wood, R.H.1    Thompson, P.T.2
  • 32
    • 0029897657 scopus 로고    scopus 로고
    • Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR
    • Yi Q, Baker D. 1996. Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR. Protein Sci 5:1060-1066.
    • (1996) Protein Sci , vol.5 , pp. 1060-1066
    • Yi, Q.1    Baker, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.