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.
出处
《计算机与应用化学》
CAS
CSCD
北大核心
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)
关键词
Α-淀粉酶
抑制剂
温度
分子动力学
Alpha-amylase, inhibitor, temperature, molecular dynamics
