室温下的小蛋白折叠研究  

INSIGHTS INTO FOLDING SIMULATION OF A MINIATURE PROTEIN AT ROOM TEMPERATURE

作　　者：孙淑臻[1] 段莉莉[1] 张庆刚[1] 

机构地区：[1]山东师范大学物理与电子科学学院,济南250014

出　　处：《山东师范大学学报（自然科学版）》2011年第4期27-29,共3页Journal of Shandong Normal University(Natural Science)

基　　金：国家自然科学基金资助项目（10874104）;中国博士后科学基金资助项目（20110490163）.

摘　　要：目前，无论在实验还是理论研究方面，研究蛋白质的从头折叠即使是小蛋白的折叠也非常困难．在室温下研究蛋白质的折叠过程可以有效的阐述蛋白质折叠机制．笔者从219M的线性结构出发，在室温下运行了15ns的分子动力学模拟，发现它在6．4ns时成功折叠到了天然态结构，此时的结构与天然态结构的均方根偏差为1．17h，模拟结构与天然态结构符合的非常好．折叠过程是首先在C端出现了螺旋，随后N端又出现了螺旋，然后螺旋从N端鱼贯式生成，最终形成天然态结构．Ab initio protein folding remains a difficult task to both experimentalists and theoreticians even for small proteins. The study folding mechanism clearly. of a protein folding process under room temperature can be used to elaborate protein In this report, starting from a fully extended structure of 219M, we have conducted a 15ns molecular dynamics （MD） simulation of 219M （PDB entry） at room temperature. We have found that it successfully folds into the native state with the minimal main - chain root - mean - square deviation （RMSD） relative to NMR structure of 1.17A at 6.4ns, the folding state and native state meet very well. The folding process of the peptide is that the helix appears in C - terminal at first, later the other end N - terminal is generated, and then the helix appears by filed type, finally it folds into the native state.

关 键 词：蛋白质折叠 219M 均方根偏差(RMSD) 自然接触比例 

分 类 号：O561.5[理学—原子与分子物理]