朊蛋白去折叠的全原子分析  

Atomistic Analysis of Prion Protein Unfolding

作　　者：和二斌 秦聪 唐佳 龙德 韩成凤 林玉铭 HE Er-bin;QIN Cong;TANG Jia;Long De;HAN Cheng-feng;LIN Yu-ming(College of Physics and Telecommunications Engineering,Yunlin Normal University,Yulin,Guangxi 537000)

机构地区：[1]玉林师范学院物理与电信工程学院

出　　处：《玉林师范学院学报》2019年第2期47-51,共5页Journal of Yulin Normal University

基　　金：玉林师范学院高层次人才科研启动项目(G2017005);国家级大学生创新创业训练启动项项目(201810606053)

摘　　要：朊病毒疾病是一种致命且具有高度传染性的神经退行性疾病,其主要特征表现为正常细胞的朊蛋白错误折叠为致病的朊蛋白形态。在本研究中,我们采用分子动力学模拟的方法,对朊蛋白在550 K高温下的去折叠行为进行了统计分析。结果表明,朊蛋白的去折叠过程以一种去折叠路径为主,其去折叠事件的发生顺序依赖于其内部疏水残基的分布。该研究揭示了朊蛋白在去折叠过程中存在的中间态及其结构特征。Prion disease is a deadly and highly contagious neurodegenerative disease,the main characteristic of which is the abnormal folding of prion protein in normal cells into pathogenic prion protein morphology.In this study,we used molecular dynamics simulation to make a statistical analysis of the folding behavior of prion protein at 550 K high temperature.The results show that the folding process of prion protein is dominated by a folding path,and the order of its folding events depends on the distribution of its internal hydrophobic residues.This study revealed the intermediate state of prion protein in the process of unfolding and its structural characteristics.

关 键 词：朊蛋白 去折叠 温度 动力学模拟 

分 类 号：Q615[生物学—生物物理学]