Universal model for α-helix and β-sheet structures in protein

被引：16

作者：

Chen, JZY ^{[1
]}

Imamura, H ^{[1
]}

机构：

[1] Univ Waterloo, Dept Phys, Waterloo, ON N2L 3G1, Canada

来源：

PHYSICA A-STATISTICAL MECHANICS AND ITS APPLICATIONS | 2003年 / 321卷 / 1-2期

关键词：

protein secondary structures; alpha helix; beta sheet; structural formation; structural transition;

D O I：

10.1016/S0378-4371(02)01789-2

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We present a unified potential-energy model that successfully reproduces the hydrogen bonding effect in proteins and can be used to represent well-defined secondary structures, both alpha-helices and beta-sheets. The native structures of the model contain both alpha-helices and beta-sheets and are entirely dependent on the sequence of the modelled protein. The model provides structural insight into the physical mechanism of such problems as structural conversion due to mutation and double native conformations with different alpha-helix and beta-sheet contents. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：181 / 188

页数：8

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