同源α-螺旋结构蛋白质Im7和Im9的变性及折叠特性的研究  

THE STUDY ON THE FEATURES OF UNFOLDING AND FOLDING FOR THE HOMOLOGOUS FOUR-HELIX PROTEINS Im?7 AND Im?9

作　　者：萨楚尔夫[1] 罗辽复[2] 

机构地区：[1]内蒙古师范大学物理系,内蒙古呼和浩特010022 [2]内蒙古大学理工学院物理系,内蒙古呼和浩特010021

出　　处：《内蒙古师范大学学报（自然科学汉文版）》2003年第4期336-339,共4页Journal of Inner Mongolia Normal University(Natural Science Edition)

基　　金：国家自然科学基金资助项目(90103030)

摘　　要：Im7和Im9是具有相似三维空间结构的同源蛋白质分子,这两种蛋白质的一级序列中有60%的残基成分相同.研究结果显示,Im7和Im9分子具有不同的稳定性和经历不同的折叠途径.为解释有关的实验事实,利用吸附反应动力学方法,分析了Im7和Im9两种蛋白质的变性过程和重折叠过程.结合Im7蛋白质和Im9蛋白质所具有的空间结构特性,对Im7和Im9蛋白质具有不同稳定特性和折叠途径存在差异的原因做了进一步的讨论和解释.The homologous four-helix proteins Im?7 and Im?9 have the same three-dimensional structure and are 60% identical in sequence.The experimental results show that Im?7 and Im?9 have different stability and appear to fold by different pathway.In order to explain the above experimental facts,here the unfolding and folding process for proteins (Im?7 and Im?9) are analyzed by means of adsorption kinetics.Considering the features of the spatial structures for the homologous proteins Im?7 and Im?9,the reasons that proteins Im?7 and Im?9 have different stability and there are the differences in folding pathway for the above proteins have been discussed and explained.

关 键 词：同源蛋白质 折叠途径 构象稳定性 吸附反应动力学 空间结构 螺旋结构蛋白质 

分 类 号：Q51[生物学—生物化学]