Protein Hydration Waters Are Susceptible to Unfavorable Perturbations.

  title={Protein Hydration Waters Are Susceptible to Unfavorable Perturbations.},
  author={Nicholas B Rego and E Paris Xi and Amish J. Patel},
  journal={Journal of the American Chemical Society},
  volume={141 5},
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… 

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