肌红蛋白力致去折叠的全原子分析  

Atomistic Analysis of Myoglobin Mechanical Unfolding

作　　者：和二斌 罗志荣[1] 朱留华[1] HE Erbin;LUO Zhirong;ZHU Liuhua(Guangxi Universities Key Lab of Complex System Optimization and Big Data Processing,College of Physical Science&Technology Engineering,Yulin Normal University,Yulin,Guangxi 531000,China)

机构地区：[1]玉林师范学院物理科学与工程技术学院,广西高校复杂系统优化与大数据处理重点实验室,广西玉林537000

出　　处：《计算物理》2020年第2期205-211,共7页Chinese Journal of Computational Physics

基　　金：Supported by the High-level Personnel Scientific Research Startup Foundation of Yulin Normal University(G2017005);the National Natural Science Foundation of China(51561031);the Natural Science Foundation of Guangxi(2016GXNSFAA380202)。

摘　　要：位于脊椎动物骨骼肌中的肌红蛋白在生命过程中扮演着重要角色,其折叠过程依赖于血红素的绑定.本文着重于肌红蛋白在力的作用下去折叠过程的全原子统计分析.结果表明血红素不仅具有生物学上的功能,而且决定其去折叠的动力学过程.在血红素不存在的情况下,肌红蛋白的力致去折叠过程存在一个中间态,其构象不同于化学变性剂所导致的去折叠中间态,发现新的中间态.结论与相关实验结果相符,揭示了肌红蛋白力致去折叠的一般机制.Myoglobin,which exists widely in skeletal muscle of vertebrates,plays crucial roles in life processes. Its proper folding depends on the binding of heme. In this paper,we report an atomistic and statistical analysis of force-induced unfolding of myoglobin with and without heme binding. It shows that heme is responsible for not only its biological functions,but also its unfolding dynamics. The unfolding pathway of myoglobin without heme binding involve an intermediate configuration. More importantly,it shows that intermediate state in force-induced unfolding process is different from that in chemical denaturant,which leads to the discovery of new intermediate configurations. Our results are in good agreement with related experimental observations and provide significant insight into general mechanisms of myoglobin unfolding.

关 键 词：肌红蛋白 机械力 血红素 分子动力学模拟 

分 类 号：Q615[生物学—生物物理学]