Simulation and Modeling of Crowding Effects on the Thermodynamic and Kinetic Properties of Proteins with Atomic Details.
Simulation and Modeling of Crowding Effects on the Thermodynamic and Kinetic Properties of Proteins with Atomic Details.
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DOI：
10.1007/s12551-013-0101-7
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发表时间：
2013-06-01
影响因子：
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通讯作者：
Qin, Sanbo
中科院分区：
文献类型：
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作者：
Zhou, Huan-Xiang;Qin, Sanbo
拥挤溶液中蛋白质折叠和结合的实验研究表明，拥挤剂对蛋白质的热力学和动力学性质有着微妙的影响。虽然一些拥挤效应可以从蛋白质的简单模型中定性地理解，但这些效应的定量合理化需要蛋白质分子的原子论表示来模拟它们与拥挤者的相互作用。一种被称为后处理的计算方法为拥挤效应的原子模型打开了大门。本文综述了后处理方法在研究拥挤效应对蛋白质折叠、构象转变和结合的热力学和动力学影响方面的应用。在拥挤的解决方案与实验的原子模型的集成承诺在细胞环境中的生化过程的新见解。
Recent experimental studies of protein folding and binding under crowded solutions suggest that crowding agents exert subtle influences on the thermodynamic and kinetic properties of the proteins. While some of the crowding effects can be understood qualitatively from simple models of the proteins, quantitative rationalization of these effects requires an atomistic representation of the protein molecules in modeling their interactions with crowders. A computational approach, known as postprocessing, has opened the door for atomistic modeling of crowding effects. This review summarizes the applications of the postprocessing approach for studying crowding effects on the thermodynamics and kinetics of protein folding, conformational transition, and binding. The integration of atomistic modeling with experiments in crowded solutions promises new insight into biochemical processes in cellular environments.