Protein Hydration Waters Are Susceptible to Unfavorable Perturbations
Protein Hydration Waters Are Susceptible to Unfavorable Perturbations
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DOI：
10.1021/jacs.8b11448
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发表时间：
2019-02-06
影响因子：
15
通讯作者：
Patel, Amish J.
中科院分区：
文献类型：
--
作者：
Rego, Nicholas B.;Xi, Erte;Patel, Amish J.
蛋白质的相互作用，它的相行为，最终，它的功能能力都受到蛋白质与其水合水之间相互作用的影响。在这里，我们研究了各种大小、形状、化学和生物功能的蛋白质，并利用分子模拟和增强采样技术表征了它们与水合水的相互作用。我们发现，类似于扩展的疏水表面，蛋白质将它们的水合水置于脱湿过渡的边缘，使它们容易受到不利的扰动。我们还发现，在这里研究的所有蛋白质中，触发脱湿所需的不利电位的强度大致相同，主要取决于被扰动的水合壳的宽度。我们的发现建立了一个框架，系统地分类蛋白质贴片根据他们如何有利地与水相互作用。
The interactions of a protein, its phase behavior, and, ultimately, its ability to function are all influenced by the interactions between the protein and its hydration waters. Here, we study proteins with a variety of sizes, shapes, chemistries, and biological functions and characterize their interactions with their hydration waters using molecular simulations and enhanced sampling techniques. We find that, akin to extended hydrophobic surfaces, proteins situate their hydration waters at the edge of a dewetting transition, making them susceptible to unfavorable perturbations. We also find that the strength of the unfavorable potential needed to trigger dewetting is roughly the same for all proteins studied here and depends primarily on the width of the hydration shell being perturbed. Our findings establish a framework for systematically classifying protein patches according to how favorably they interact with water.