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Volumn 114, Issue 16, 2001, Pages 7267-7273

Hierarchy of events in the folding of model proteins

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; ENERGY GAP; GROUND STATE; LATTICE CONSTANTS; MATHEMATICAL MODELS; MONTE CARLO METHODS; PHASE TRANSITIONS; PROBABILITY DISTRIBUTIONS;

EID: 0035932720     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.1361076     Document Type: Article
Times cited : (44)

References (56)
  • 13
    • 0032874909 scopus 로고    scopus 로고
    • R. A. Broglia, G. Tiana, S. Pasquali, H. E. Roman, and E. Vigezzi, Proc. Natl. Acad. Sci. U.S.A. 95, 12930 (1998); 96, 10943 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10943
  • 16
    • 6644221243 scopus 로고    scopus 로고
    • cond-mat/0005150 (to be published)
    • R. A. Broglia and G. Tiana, cond-mat/0005150 (to be published).
    • Broglia, R.A.1    Tiana, G.2
  • 29
    • 6644221844 scopus 로고    scopus 로고
    • note
    • Within the present scenario of protein folding the question of the relative importance of local vs nonlocal contacts (cf. e.g., Refs. 21, 29, and 30 and references therein) is somewhat transcended. In fact, they become complementary expressions of the same reality.
  • 38
    • 6644227715 scopus 로고    scopus 로고
    • note
    • c is essentially identical.
  • 45
    • 6644225848 scopus 로고    scopus 로고
    • note
    • Local elementary structures involve very few monomers. Consequently it is difficult to associate them to macroscopic measurable quantities and, in general, to detect them directly from experiment, except if their formation is associated with a local minimum of the overall energy (for example, "three-state folding"). On the other hand, the monomers participating in the formation of LES are among the strongest interacting amino acids. A possible way to learn about LES, is to perform protein engineering experiments (Refs. 31 and 45).
  • 52
    • 6644221843 scopus 로고    scopus 로고
    • note
    • The average is performed only over mutations which do not prevent folding.
  • 53
    • 6644228058 scopus 로고    scopus 로고
    • note
    • 36 has a very low energy in the structure chosen as native. It is possible that nature selects less optimized sequences and that mutations in real proteins decrease folding time. In any case, the change in folding time associated with point mutations in hot sites (either positive or negative) is much larger than that associated with mutations in cold or warm sites.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.