Protein Hydration Waters Are Susceptible to Unfavorable Perturbations

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 inter...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2019-02, Vol.141 (5), p.2080-2086
Main Authors: Rego, Nicholas B, Xi, Erte, Patel, Amish J
Format: Article
Language:English
Subjects:
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Proteins - chemistry
Surface Properties
Water - chemistry
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.8b11448