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Volumn 113, Issue 17, 2000, Pages 7702-7711

Time scales and pathways for kinetic energy relaxation in solvated proteins: Application to carbonmonoxy myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

ANELASTIC RELAXATION; DAMPING; FRICTION; KINETIC ENERGY; MATHEMATICAL MODELS; MOLECULAR STRUCTURE; SOLVENTS; VISCOSITY;

EID: 0034321095     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.1313554     Document Type: Article
Times cited : (96)

References (45)
  • 31
    • 14344282985 scopus 로고    scopus 로고
    • note
    • It is natural to suggest that internal viscosity should play a role in the dynamics of proteins (and other macromolecules). To a first approximation, any relaxation process in proteins can be described in terms of suitable reaction coordinates (a small number) along which the dynamics is nonlinear. The rest of the degrees of freedom constitute the "bath." Because the polypetide chain is, for all practical purposes, "macroscopic," the spectrum of the "bath" can be approximated as a continuum. Such a reduced description can be mathematically captured by the GLE [Eq. (1)] (Ref. 45).
  • 43
    • 14344274738 scopus 로고    scopus 로고
    • note
    • 3 ≃ 2.2. Thus in this mechanism internal viscosity is related to loop entropy.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.