메뉴 건너뛰기




Volumn 259, Issue 5, 1996, Pages 988-994

Local interactions dominate folding in a simple protein model

Author keywords

Lattice models; Local interactions; Protein folding

Indexed keywords

PROTEIN;

EID: 0030604696     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0375     Document Type: Article
Times cited : (93)

References (22)
  • 1
    • 0028024928 scopus 로고
    • Specific nucleus as a transition state for protein folding: An evidence from lattice model
    • Abkevich, V. I., Gutin, A. M. & Shakhnovich, E. I. (1994). Specific nucleus as a transition state for protein folding: an evidence from lattice model. Biochemistry, 33, 10026-10036.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 2
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J. D. & Wolynes, P. G. (1987). Spin glasses and the statistical mechanics of protein folding. Proc. Natl Acad. Sci. USA, 84, 7524-7528.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 3
    • 0028941444 scopus 로고
    • Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor
    • Camacho, C. J. & Thirumalai, D. (1995). Theoretical predictions of folding pathways by 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
  • 4
    • 0028929204 scopus 로고
    • Kinetics of protein folding
    • Chan, H. S. (1995). Kinetics of protein folding. Nature, 373, 664-665.
    • (1995) Nature , vol.373 , pp. 664-665
    • Chan, H.S.1
  • 5
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and hetropolymers
    • Chan, H. S. & Dill, K. A. (1994). Transition states and folding dynamics of proteins and hetropolymers. J. Chem. Phys. 100, 9238-9257.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 0027364930 scopus 로고
    • Dissecting the structure of a partially folded protein: Circular dichroism and nuclear magnetic resonance studies of peptides of ubiquitin
    • Cox, J. P. L., Evans, P. A., Packman, L. C., Williams, D. H. & Woolfson, D. N. (1995). Dissecting the structure of a partially folded protein: circular dichroism and nuclear magnetic resonance studies of peptides of ubiquitin. J. Mol. Biol. 220, 483-492.
    • (1995) J. Mol. Biol. , vol.220 , pp. 483-492
    • Cox, J.P.L.1    Evans, P.A.2    Packman, L.C.3    Williams, D.H.4    Woolfson, D.N.5
  • 7
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 9
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins: Models for initiation of protein folding. II. Plastocyanin
    • Dyson, H. L., Sayre, J. R., Merututka, G., Shin, H. C., Lerner, R. A. & Wright, P. E. (1992). Folding of peptide fragments comprising the complete sequence of proteins: models for initiation of protein folding. II. Plastocyanin. J. Mol. Biol. 226, 819-835.
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.L.1    Sayre, J.R.2    Merututka, G.3    Shin, H.C.4    Lerner, R.A.5    Wright, P.E.6
  • 10
    • 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
    • 0025906759 scopus 로고
    • An analysis of protein folding pathways
    • Moult, J. & Unger, R. (1991). An analysis of protein folding pathways. Biochemistry, 30, 3816-3824.
    • (1991) Biochemistry , vol.30 , pp. 3816-3824
    • Moult, J.1    Unger, R.2
  • 14
  • 15
    • 0028270634 scopus 로고
    • Kinetics of protein folding. A lattice model study of the requirements for folding to the native state
    • Šali, A., Shakhnovich, E. & Karplus, M. (1994b). Kinetics of protein folding. A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235, 1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Šali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 16
    • 0026563495 scopus 로고
    • The folding of an enzyme. VI. The folding pathway of barnase: Comparison with theoretical models
    • Serrano, L., Matouschek, A. & Fersht, A. R. (1992). The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models. J. Mol. Biol. 224, 847-859.
    • (1992) J. Mol. Biol. , vol.224 , pp. 847-859
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 17
    • 0025146274 scopus 로고
    • Implications of thermodynamics of protein folding for evaluation of primary sequences
    • Shakhnovich, E. & Gutin, A. (1990a). Implications of thermodynamics of protein folding for evaluation of primary sequences. Nature, 346, 773-775.
    • (1990) Nature , vol.346 , pp. 773-775
    • Shakhnovich, E.1    Gutin, A.2
  • 18
    • 36549097257 scopus 로고
    • Enumeration of all compact conformation of copolymers with random sequence of links
    • Shakhnovich, E. & Gutin, A. (1990b). Enumeration of all compact conformation of copolymers with random sequence of links. J. Chem. Phys. 93, 5967-5971.
    • (1990) J. Chem. Phys. , vol.93 , pp. 5967-5971
    • Shakhnovich, E.1    Gutin, A.2
  • 20
    • 0007725036 scopus 로고
    • Folding kinetics of proteinlike hetropolymers
    • Socci, N. D. & Onuchic, J. N. (1994). Folding kinetics of proteinlike hetropolymers. J. Chem. Phys. 101, 1519-1528.
    • (1994) J. Chem. Phys. , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 22
    • 0015597839 scopus 로고
    • Nucleation, rapid folding, and globular interchain regions in proteins
    • Wetlaufer, D. B. (1973). Nucleation, rapid folding, and globular interchain regions in proteins. Proc. Natl Acad. Sci. USA, 70, 697-701.
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.