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

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.