生物信息学
生化工程
破译
计算生物学
适应(眼睛)
计算机科学
功能(生物学)
理论(学习稳定性)
蛋白质稳定性
化学
材料科学
纳米技术
生物
生物信息学
工程类
遗传学
生物化学
基因
机器学习
神经科学
作者
Štěpán Timr,Dominique Madern,Fabio Sterpone
出处
期刊:Progress in Molecular Biology and Translational Science
日期:2020-01-01
卷期号:: 239-272
被引量:14
标识
DOI:10.1016/bs.pmbts.2019.12.007
摘要
Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors underlying the resistance of proteins to the thermal stress has important consequences. First of all, it can aid the design of thermostable enzymes able to perform efficient catalysis in the high-temperature regime. Second, it is an essential brick of knowledge required to decipher the evolutionary pathways of life adaptation on Earth. Thanks to the development of atomistic simulations and ad hoc enhanced sampling techniques, it is now possible to investigate this problem in silico, and therefore provide support to experiments. After having described the methodological aspects, the chapter proposes an extended discussion on two problems. First, we focus on thermophilic proteins, a perfect model to address the issue of thermal stability and molecular evolution. Second, we discuss the issue of how protein thermal stability is affected by crowded in vivo-like conditions.
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