Water dynamics clue to key residues in protein folding
Water dynamics clue to key residues in protein folding
复制标题
水动力学揭示蛋白质折叠中关键残基
DOI：
10.1016/j.bbrc.2010.01.003
复制
发表时间：
2010-01-29
影响因子：
3.1
通讯作者：
She, Zhen-Su
中科院分区：
文献类型：
--
作者：
Gao, Meng;Zhu, Huaiqiu;She, Zhen-Su
从水化水动力学的研究出发，提出了一种不依赖于实验蛋白质结构信息的计算方法来识别蛋白质折叠中的关键残基。基于全原子分子动力学模拟，识别了Trp笼蛋白折叠过程中具有不同水动力学行为的两个关键残基。所确定的关键残基显示在3D结构和疏水诱导的崩溃中起着至关重要的作用。通过对关键残基周围水化水动力学的观察，可以解释折叠的动力学途径。(C)2010年爱思唯尔公司All rights reserved.
A computational method independent of experimental protein structure information is proposed to recognize key residues in protein folding, from the Study of hydration water dynamics. Based on all-atom molecular dynamics simulation, two key residues are recognized with distinct water dynamical behavior in a folding process of the Trp-cage protein. The identified key residues are shown to play an essential role in both 3D structure and hydrophobic-induced collapse. With observations on hydration water dynamics around key residues, a dynamical pathway of folding can be interpreted. (C) 2010 Elsevier Inc. All rights reserved.