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Volumn 5, Issue 9, 1996, Pages 1826-1832

Denaturants can accelerate folding rates in a class of globular proteins

Author keywords

denaturants; energy landscape; folding rates; lattice model

Indexed keywords

GLOBULAR PROTEIN;

EID: 0029786704     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050908     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 36448999595 scopus 로고
    • Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice model simulations
    • Abkevich VI, Gutin AM, Shakhnovich EI 1994. 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) J Chem Phys , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 2
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso DOV, Dill KA. 1991. Solvent denaturation and stabilization of globular proteins. Biochemistry 30:5974-5985.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.O.V.1    Dill, K.A.2
  • 3
    • 0027245421 scopus 로고
    • Three state analysis of sperm whale apomyoglobin folding
    • Barrick D, Baldwin RL. 1993 Three state analysis of sperm whale apomyoglobin folding. Biochemistry 32:3790-3796.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 5
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho CJ, Thirumalai D, 1993. Kinetics and thermodynamics of folding in model proteins. Proc Natl Acad Sci USA 90:6369-6372.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 6
    • 0029028698 scopus 로고
    • Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways
    • Camacho CJ, Thirumalai D. 1995a. Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways. Proteins Struct Funct Genet 22:27-40.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 27-40
    • Camacho, C.J.1    Thirumalai, D.2
  • 7
    • 0028941444 scopus 로고
    • Theoretical predictions of folding pathways using the proximity rule, with applications to bovine pancreatic trypsin inhibitor
    • Camacho CJ, Thirumalai D. 1995b. Theoretical predictions of folding pathways using the proximity rule, with applications to bovine pancreatic trypsin inhibitor Proc Natl Acad Sci USA 92 1277-1281.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1277-1281
    • Camacho, C.J.1    Thirumalai, D.2
  • 8
    • 0017815610 scopus 로고
    • Experimental studies of protein folding and unfolding
    • Creighton TE. 1978. Experimental studies of protein folding and unfolding. Prog Biophys Mol Biol 33:231-297.
    • (1978) Prog Biophys Mol Biol , vol.33 , pp. 231-297
    • Creighton, T.E.1
  • 9
    • 0026537987 scopus 로고
    • The disulfide folding pathway of BPTI
    • Creighton TE. 1992. The disulfide folding pathway of BPTI. Science 256:111-112.
    • (1992) Science , vol.256 , pp. 111-112
    • Creighton, T.E.1
  • 11
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • Greene RF, Pace CN. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 249:5388-5393.
    • (1974) J Biol Chem , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 12
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales and pathways
    • Guo Z, Thirumalai D. 1995. Kinetics of protein folding: Nucleation mechanism, time scales and pathways. Biopolymers 36:83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 13
    • 0022471054 scopus 로고
    • Effects of guanidine hydrochloride on the refolding kinetics of denatured thioridazine
    • Kelley RF, Wilson J, Bryant C, Stellwagen E. 1986. Effects of guanidine hydrochloride on the refolding kinetics of denatured thioridazine. Biochemistry 25:728-732.
    • (1986) Biochemistry , vol.25 , pp. 728-732
    • Kelley, R.F.1    Wilson, J.2    Bryant, C.3    Stellwagen, E.4
  • 14
    • 0026584375 scopus 로고
    • Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate
    • Kiefhaber T, Grunert HP, Hahn U, Schmid FX. 1992. Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate. Proteins Struct Funci Genet 12:171-179.
    • (1992) Proteins Struct Funci Genet , vol.12 , pp. 171-179
    • Kiefhaber, T.1    Grunert, H.P.2    Hahn, U.3    Schmid, F.X.4
  • 15
    • 0019324434 scopus 로고
    • Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B
    • McCoy LF, Rowe ES, Wong KP. 1980. Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B. Biochemistry 19:4738-4743.
    • (1980) Biochemistry , vol.19 , pp. 4738-4743
    • McCoy, L.F.1    Rowe, E.S.2    Wong, K.P.3
  • 19
    • 0039224962 scopus 로고
    • Role of proline peptide band isomerization in unfolding and refolding ribonuclease
    • Schmid FX, Grafl R, Wrba A, Beintama JJ. 1986. Role of proline peptide band isomerization in unfolding and refolding ribonuclease. Proc Natl Acad Sci USA 83:872-876
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 872-876
    • Schmid, F.X.1    Grafl, R.2    Wrba, A.3    Beintama, J.J.4
  • 20
    • 0027050824 scopus 로고
    • Modeling the effects of mutations on the denatured states of proteins
    • Shortle D, Chan HS, Dill KA. 1992. Modeling the effects of mutations on the denatured states of proteins. Protein Sci 1:201-215
    • (1992) Protein Sci , vol.1 , pp. 201-215
    • Shortle, D.1    Chan, H.S.2    Dill, K.A.3
  • 21
    • 0007725036 scopus 로고
    • Folding kinetics of protein-like heteropolymers
    • Socci ND, Onuchic JN. 1994. Folding kinetics of protein-like heteropolymers. J Chem Phys 101:1519-1528.
    • (1994) J Chem Phys , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 22
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of protein like heteropolymers: Monte Carlo histogram technique
    • Socci ND, Onuchic JN. 1995. Kinetic and thermodynamic analysis of protein like heteropolymers: Monte Carlo histogram technique. J Chem Phys 103:4732-4744.
    • (1995) J Chem Phys , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 23
    • 0014718113 scopus 로고
    • Protein denaturation: Theoretical models for the mechanism of denaturation
    • Tanford C. 1970. Protein denaturation: Theoretical models for the mechanism of denaturation. Adv Protein Chem 24:1-95.
    • (1970) Adv Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 24
    • 9544257077 scopus 로고
    • Monte Carlo calculations on the dynamics of polymers in dilute solution
    • Verdier PH, Stockmeyer WH. 1967. Monte Carlo calculations on the dynamics of polymers in dilute solution. J Chem Phys 36:277-285.
    • (1967) J Chem Phys , vol.36 , pp. 277-285
    • Verdier, P.H.1    Stockmeyer, W.H.2
  • 25
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman JS, Kim PS. 1991. Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253:1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 26
    • 0026537987 scopus 로고
    • The disulfide folding pathway of BPTI: Response
    • Weissman JS, Kim PS. 1992 The disulfide folding pathway of BPTI: Response. Science 256:112-114.
    • (1992) Science , vol.256 , pp. 112-114
    • Weissman, J.S.1    Kim, P.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.