热稳定性
普鲁兰酶
蛋白质工程
热稳定性
分子动力学
酶
淀粉
化学
生物化学
计算生物学
生物系统
生化工程
材料科学
计算机科学
生物
计算化学
有机化学
工程类
作者
Jianxiu Li,Shuqing Wang,Qiang Du,Hang Wei,Xiaoming Li,Meng Ju,Qingyan Wang,Neng-Zhong Xie,Ribo Huang,Kuo‐Chen Chou
标识
DOI:10.2174/1381612824666181113120948
摘要
Background: The relationship between protein structure and its bioactivity is one of the fundamental problems for protein engineering and pharmaceutical design. Method: A new method, called SPTD (Simulated Protein Thermal Detection), was proposed for studying and improving the thermal stability of enzymes. The method was based on the evidence observed by conducting the MD (Molecular Dynamics) simulation for all the atoms of an enzyme vibrating from the velocity at a room temperature (e.g., 25°C) to the desired working temperature (e.g., 65°C). According to the recorded MD trajectories and the coordinate deviations of the constituent residues under the two different temperatures, some new strategies have been found that are useful for both drug delivery and starch industry. Conclusion: The SPTD technique presented in this paper may become a very useful tool for pharmaceutical design and protein engineering.
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