Protein Hydration Thermodynamics: The Influence of Flexibility and Salt on Hydrophobin II Hydration
Protein Hydration Thermodynamics: The Influence of Flexibility and Salt on Hydrophobin II Hydration
复制标题
蛋白质水合热力学：柔韧性和盐对疏水蛋白 II 水合的影响
DOI：
10.1021/acs.jpcb.7b12060
复制
发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Patel, Amish J.
中科院分区：
文献类型：
--
作者：
Remsing, Richard C.;Xi, Erte;Patel, Amish J.
蛋白质和其他大分子溶质的溶解度在许多生物、化学和医学过程中发挥着重要作用。蛋白质溶解度的一个重要决定因素是蛋白质的溶剂化自由能，它量化了蛋白质与其周围的水溶液之间相互作用的总体强度。在这里，我们提出了一个全原子显式溶剂计算框架，用于快速估计蛋白质溶剂化自由能。使用这个框架，我们以计算有效的方式估计了疏水蛋白 II（一种两亲性真菌蛋白）的水合自由能。我们进一步探讨了增强柔韧性和添加氯化钠如何影响蛋白质水合自由能，并发现在这两种情况下蛋白质水合自由能都会增加，从而使蛋白质水合变得不太有利。
The solubility of proteins and other macromolecular solutes plays an important role in numerous biological, chemical, and medicinal processes. An important determinant of protein solubility is the solvation free energy of the protein, which quantifies the overall strength of the interactions between the protein and the aqueous solution that surrounds it. Here we present an all-atom explicit-solvent computational framework for the rapid estimation of protein solvation free energies. Using this framework, we estimate the hydration free energy of hydrophobin II, an amphiphilic fungal protein, in a computationally efficient manner. We further explore how the protein hydration free energy is influenced by enhancing flexibility and by the addition of sodium chloride, and find that it increases in both cases, making protein hydration less favorable.