黄粉虫α-淀粉酶与抑制剂相互作用的分子动力学模拟  

The molecular dynamics simulation of the interaction between the tenebrio moilitor alpha-amylase and its inhibitor

作　　者：朱志飞 徐祖民 宁婷婷 王正武 张革新 马延和[2] 

机构地区：[1]江南大学化学与材料工程学院,江苏无锡214122 [2]中国科学院微生物研究所,北京100080

出　　处：《计算机与应用化学》2007年第8期1029-1032,共4页Computers and Applied Chemistry

基　　金：国家"973"计划(2003CB716001;2004CB719605);工业生物技术教育部重点实验室课题(KLIB-ZR200503)

摘　　要：α-淀粉酶与抑制剂相互作用一直受到人们关注。本文利用hyperchem 7.5软件,在opls力场下,选择分子动力学方法,模拟了不同温度条件下,黄粉虫的α-淀粉酶与抑制剂相互作用。通过对势能数据分析,结果显示在280 K左右黄粉虫的α-淀粉酶与抑制剂相互作用最强。这与实验得出的最适温度较为吻合。The interaction between alpha-amylase and its inhibitor is a focus. In this paper, molecular dynamics simulation of the interaction between the tenebrio mollitor alpha-amylase and its inhibitor at different temperature was carried out with opls force field by hyperchem 7.5 soft. Analyzed the potential energy data, interaction between alpha-amylase and its inhibitor is the strongest at about 280 K. The result is similar to experimental optimal temperature.

关 键 词：Α-淀粉酶 抑制剂 温度 分子动力学 

分 类 号：O647.31[理学—物理化学] Q71[理学—化学]