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Protein folding dynamics via quantification of kinematic energy landscape.

Identifieur interne : 002D00 ( Main/Curation ); précédent : 002C99; suivant : 002D01

Protein folding dynamics via quantification of kinematic energy landscape.

Auteurs : Sëma Kachalo [États-Unis] ; Hsiao-Mei Lu ; Jie Liang

Source :

RBID : pubmed:16487000

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English descriptors

Abstract

We study folding dynamics of proteinlike sequences on a square lattice using a physical move set that exhausts all possible conformational changes. By analytically solving the master equation, we follow the time-dependent probabilities of occupancy of all 802 075 conformations of 16 mers over 7 orders of time span. We find that (i) folding rates of these proteinlike sequences of the same length can differ by 4 orders of magnitude, (ii) folding rates of sequences of the same conformation can differ by a factor of 190, and (iii) parameters of the native structures, designability, and thermodynamic properties are weak predictors of the folding rates; rather, a basin analysis of the kinematic energy landscape defined by the moves can provide an excellent account of the observed folding rates.

DOI: 10.1103/PhysRevLett.96.058106
PubMed: 16487000

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pubmed:16487000

Le document en format XML

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