کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1934755 | 1050650 | 2008 | 5 صفحه PDF | دانلود رایگان |
A “key-residue” hypothesis that a few residues’ characteristics contain the essential dynamics of the whole protein is proposed for the study of side-chain relaxation near native states. Molecular dynamics simulation is performed on the folding of Trp-cage, and four key residues are discovered and shown to be highly sensitive to the change of state of the protein away from the native state. Order parameters that characterize the geometrical properties of key residues are shown to form valuable phase plane on which one distinguishes different reaction pathways. Furthermore, one of the key residues, Trp6, is observed to display two reconfiguration processes, in which one is induced by an unconstrained torsion of the side-chain of Trp6, with a rate faster by almost an order of magnitude than the other one described by Kussell’s model. The faster process seems to occur more frequently in our simulation and thus represent a significant mechanism in folding dynamics.
Journal: Biochemical and Biophysical Research Communications - Volume 373, Issue 1, 15 August 2008, Pages 64–68