二氢叶酸还原酶在盐溶液中的分子动力学模拟  

Molecular dynamics simulation of dihydrofolate reductase in salt solution

作　　者：王四华[1] 付晓平[1] 王文研[1] 张光亚[1] 

机构地区：[1]华侨大学化工学院生物工程与技术系,福建厦门361021

出　　处：《计算机与应用化学》2012年第4期431-435,共5页Computers and Applied Chemistry

基　　金：国家自然科学基金资助项目(20806031);福建省自然科学基金资助项目(2009J01030);华侨大学高层次人才科研启动项目(10BS220)

摘　　要：为了研究嗜盐酶如何在高盐环境下维持稳定性与活性,本文以沃尔卡尼极嗜盐菌及大肠杆菌的二氢叶酸还原酶(DHFR)为模型,将二者分别置于5种不同盐浓度的水溶液中进行分子动力学模拟。经9ns动力学模拟,得到了二者在不同浓度盐溶液中的运动轨迹,通过对运动轨迹的分析,获取了二者在不同盐浓度下的动力学特性。结果发现嗜盐古生菌的二氢叶酸还原酶自身所形成盐桥及与溶剂所形成的氢键均比大肠杆菌的二氢叶酸还原酶多,而溶剂可及性表面则要小,二者差异均达极显著水平。同时还分析了这两种分子及其氨基酸残基的柔性等。In oder to find how halophilic enzyme maintain stability and activity in high salt concentration,dihydrofolate reductase from the Haloferax volcanii and Escherichia coli has been chosen as an model respectively, and suffer molecular dynamics simulation in five different concentration of salt solution. Molecular dynamics trajectories of the dihydrofolate reductases in the five different salt solutions were obtained after 9 ns of simulation, by a detailed analysis of the trajectories, we obtain their dynamical characteristics in different salt solution. The results showed that the salt bridge and protein-solvent H-bond of dihydrofolate reductase from the Haloferax volcanii are significantly more than that of dihydrofolate reduetase from Escherichia coli, while the solvent accessible surface area of dihydrofolate reductase from the Escherichia coli is significantly large than that of dihydrofolate reductase from the Haloferax volcanii, The RMSD and each amino acids RMSF value were also addressed.

关 键 词：分子动力学模拟 二氢叶酸还原酶 嗜盐机理 溶剂可及性表面 氢键 

分 类 号：TQ015.9[化学工程] TP391.9[自动化与计算机技术—计算机应用技术]