蛋白质折叠速率的Kramers理论分析  

Analysis of protein folding rates with kramers'theory

作　　者：解晓欣 张颖[1,2] 吕军 XIE Xiao-xin;ZHANG Ying;LV Jun(College of Sciences,Inner Mongolian University of Technology,Hohhot 010051,China;Inner Mongolian Key Laboratory of Statistical Analysis Theory for Life Data and Neural Network Modeling,Hohhot 010051,China)

机构地区：[1]内蒙古工业大学理学院,呼和浩特010051 [2]内蒙古自治区生命数据统计分析理论与神经网络建模重点实验室,呼和浩特010051

出　　处：《内蒙古工业大学学报（自然科学版）》2021年第2期112-119,共8页Journal of Inner Mongolia University of Technology：Natural Science Edition

基　　金：内蒙古自治区自然科学基金资助项目(2019LH01004)。

摘　　要：理解蛋白质的快速折叠机制对于现代分子生物学具有基本的重要性.以蛋白质天然态非局域接触数的1/n次幂估计折叠自由能垒高度(n为耦合振动自由度),基于弱碰撞极限情形的Kramers逃逸速率理论,得到一个蛋白质折叠速率预测模型.在包含150个蛋白质折叠速率的实验数据集上检验该模型,n=3时,模型获得了对实验值约80%的拟合度.结果表明,天然态非局域接触数是蛋白质折叠速率的决定因素之一.此外,在n=1时模型退化为拓扑异构体搜索模型.Understanding the rapid folding mechanism of proteins is of fundamental importance for modern molecular biology.In this study,we estimated the height of the free energy barrier for folding with the 1/n power of the number of non-local contacts in the natural state of the protein(n was the degree of freedom of coupling vibration),and derived a protein folding rate prediction model based on the Kramers escape rate theory of weak collision limit.This model was tested on an experimental dataset containing 150 protein folding rates.The goodness of fit was about 80%between the model and the experimental data when n=3.The results show that the number of natural non-local contacts is one of the determinants of protein folding rates.Besides,when n=1,the model degenerates into a topomer search model.

关 键 词：蛋白质折叠 速率理论 自由能垒 非局域接触 弱碰撞极限 

分 类 号：Q61[生物学—生物物理学] Q71