MD模拟研究Mini-protein Chignolin去折叠过程中残基的构象熵  

Study of Conformational Entropies of Mini-protein Chignolin During Unfolding by MD Simulation

作　　者：刘贵忠[1] 于家峰[1] 

机构地区：[1]德州学院物理系,山东德州253023

出　　处：《德州学院学报》2007年第6期1-4,共4页Journal of Dezhou University

基　　金：国家自然科学基金(90403120);山东省自然科学基金(Y2005D12)

摘　　要：采用分子动力学模拟方法,对Chignolin在260 K、300 K、350 K和400 K进行去折叠模拟,计算8个残基(2—9位点)的构象熵.研究发现,构象熵值可大致分为低熵组、中熵组和高熵组.影响残基熵值的因素主要为温度、残基的原子数、残基所在位点、与邻近残基的相互作用等.还发现残基的构象熵有短时间急剧变化——阶梯跃变的现象.这意味着蛋白质的去折叠可能是不连续的.提示蛋白质的折叠过程可能也是不连续的.The unfolding of chignonlin at 260K, 300K and 350K was carried on by MD sumulation and the entropies of 8 residues was calculated in this paper. The results show that the conformational entropies can be devided into three groups such as low, middle, and high. The factor influencing the conformational entropies of residues lie on temperature, the number of residues＇ atoms, the location of residue and the interaction with the neighboring residues. Ladder jump of the conformational entropies in short time were obtained which mean the cousrs of unfolding is discontinuous.

关 键 词：Chignolin 构象熵 分子动力学模拟 去折叠 阶梯跃变 

分 类 号：Q612[生物学—生物物理学]