%0 Journal Article
%T THE STUDY ON THE FLEXIBILITY OF INSULIN HEXAMER IN SOLUTION BY MOLECULAR DYNAMICS SIMULATIONS<br>胰岛素六聚体在水溶液中的构象柔性研究
%A WANG Wei-yan
%A LU Ben-zhuo
%A CHEN Wei-zu
%A WANG Cun-xin
%A <br>王维宴
%A 卢本卓
%A 陈慰祖
%A 王存新
%J 生物物理学报
%D 2003
%I 
%X In order to study the flexibility of insulin hexamer in solution, two 600 ps molecular dynamics (MD) simulations of the protein complex, R-state human insulin hexamer system, were carried out respectively. Through the comparison analysis for two MD simulation data, it was found that for the system with Zn2+ ions and phenol, the conformational flexibility of insulin hexamer was decreased. However, in the absence of Zn2+ and phenol, the insulin hexamer exhibits a higher degree of conformational flexibility in aqueous solution. The remarkable and rapid conformational changes of the β-sheet at C-terminus of the B-chain in every insulin monomer provide a structural basis for insulin to bind with its receptor. These results are in good agreement with the experimental observation.
%K Molecular dynamics simulation
%K Insulin hexamer
%K Conformational flexibility<br>胰岛素六聚体
%K 分子动力学模拟
%K 构象柔性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=2E6349801C668AB0&yid=D43C4A19B2EE3C0A&vid=2A8D03AD8076A2E3&iid=CA4FD0336C81A37A&sid=6209D9E8050195F5&eid=1371F55DA51B6E64&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=19