文章基本信息

标题：Understanding β-hairpin formation
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作者：Aaron R. Dinner ; Themis Lazaridis ; Martin Karplus 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1999
卷号：96
期号：16
页码：9068-9073
DOI：10.1073/pnas.96.16.9068
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The kinetics of formation of protein structural motifs (e.g., -helices and {beta}-hairpins) can provide information about the early events in protein folding. A recent study has used fluorescence measurements to monitor the folding thermodynamics and kinetics of a 16-residue {beta}-hairpin. In the present paper, we obtain the free energy surface and conformations involved in the folding of an atomistic model for the {beta}-hairpin from multicanonical Monte Carlo simulations. The results suggest that folding proceeds by a collapse that is downhill in free energy, followed by rearrangement to form a structure with part of the hydrophobic cluster; the hairpin hydrogen bonds propagate outwards in both directions from the partial cluster. Such a folding mechanism differs from the published interpretation of the experimental results, which is based on a helix-coil-type phenomenological model.
关键词：charmm ; implicit solvent ; multicanonical Monte Carlo ; protein folding