| 通过分析来自Pyrococcus abyssi的腈水解酶中带电基团位置变化探讨蛋白耐热机制 |
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| 引用本文： | 汤晓芒,张鲁嘉,崔东冰,姚志强,王学东,魏东芝.通过分析来自Pyrococcus abyssi的腈水解酶中带电基团位置变化探讨蛋白耐热机制[J].生物加工过程,2012(6):29-33. |
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| 作者姓名： | 汤晓芒 张鲁嘉 崔东冰 姚志强 王学东 魏东芝 |
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| 作者单位： | [1]华东理工大学生物反应器国家重点实验室鲁华生物技术研究所,上海200237 [2]南京工业大学材料化学工程国家重点实验室,南京210009 |
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| 基金项目： | 国家自然科学基金资助项目（31201296）;国家高技术研究发展计划（863计划）资助项目（2012AA020403）;材料化学工程国家重点实验室开放课题基金资助项目（KL10-09） |
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| 摘 要： | 蛋白含带电侧链基团的氨基酸的位置对蛋白质的热稳定性有很大的影响,目前,往往采用蛋白质结构模型"静态"分析这一影响。本文以1株耐热的腈水解酶作为研究对象,构建并异源表达了该酶,对其酶学性质进行初步分析。利用Discovery Studio对该酶进行同源建模,得到空间结构。将此空间结构利用Gromacs软件在不同温度下进行分子动力学(MD)模拟,使用Macrodox软件计算蛋白质所有带电氨基酸残基的包埋率与溶剂可接触性面积(SA),发现在不同温度下,部分氨基酸带电基团的SA值会发生显著变化。说明通过静态分析并不一定能够得到非常准确的结果,而应进行动态分析。
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| 关 键 词： | 同源建模 分子动力学 溶剂可接触性 腈水解酶 热稳定性 |
Mechanism of protein thermostability by analyzing change of ionizable group position in nitrilase from Pyrococcus abyssi |
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| TANG Xiaomang,ZHANG Lujia,CUI Dongbing,YAO Zhiqiang,WANG Xuedong,WEI Dongzhi.Mechanism of protein thermostability by analyzing change of ionizable group position in nitrilase from Pyrococcus abyssi[J].Chinese Journal of Bioprocess Engineering,2012(6):29-33. |
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| Authors: | TANG Xiaomang ZHANG Lujia CUI Dongbing YAO Zhiqiang WANG Xuedong WEI Dongzhi |
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| Institution: | 1. New World Biotechnology Institute, State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology, Shanghai 200237, China ; 2. State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing University of Technology, Nanjing 210009, China) |
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| Abstract: | The position of the amino acids with ionizable group of protein had a great effect on protein thermostability. A thermoactive nitrilase was constructed and the heterologous expressed. The basic properties were tested. The enzyme was modeled by Discovery Studio program in homology modeling protocol and simulated in Gromacs molecular dynamics program at different given temperatures. Finally,the macrodox program was used to calculate the proteins solvent accesssibility. The solvent accessibility of ionizable groups in nitrilase was different at changing temperatures. It was necessary for dynamic analysis of protein＇s themrostability mechanism. |
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| Keywords: | homology modeling molecular dynamics solvent accessibility nitrilase thermostability |
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