Minimal model for studying prion-like folding pathways

被引：9

作者：

Chen, JZY ^{[1
]}

Lemak, AS ^{[1
]}

Lepock, JR ^{[1
]}

Kemp, JP ^{[1
]}

机构：

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

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 2003年 / 51卷 / 02期

关键词：

minimal model; proteins; prion; folding pathway; Monte Carlo simulation;

D O I：

10.1002/prot.10329

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Monte Carlo technique is used to simulate the energy landscape and the folding kinetics of a minimal prion-like protein model. We show that the competition between hydrogen-bonding and hydrophobic interactions yields two energetically favored secondary structures, an alpha-helix and a beta-hairpin. Folding simulations indicate that the probability of reaching the alpha-helix form from a denatured random conformation is much higher than the probability of reaching the beta-sheet form, even though the beta-sheet has a lower energy. The existence of a lower energy beta-sheet state gives the possibility for the normal alpha-helix structure to take a structural transformation into the beta-sheet structure under external influences. (C) 2003 Wiley-Liss, Inc.

引用

页码：283 / 288

页数：6

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