期刊
CHEMICAL PHYSICS LETTERS
卷 399, 期 4-6, 页码 342-348出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cplett.2004.09.140
关键词
-
A view lacking in earlier studies on protein folding is that the process is critically influenced by the thermal motion of water molecules. Here it is pointed out that there is a powerful driving force, a large gain in the translational entropy (TE) of water, which competes with the large loss of the conformational entropy in the folding. We analyze the TE of water in which a protein molecule with a prescribed conformation is immersed. We consider a number of conformations and show that the largest TE is attained only in the native structure. (C) 2004 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据