(688d) Characterizing Protein Hydration to Inform its Interactions

The extent to which the inherent structure of water is perturbed by complex molecules, such as proteins, peptides, and surfactants, influences the thermodynamics and the kinetics of their assembly. However, accurately characterizing this perturbation is challenging, because the manner in which proteins disrupt the inherent structure of water depends not only on the chemistry of the underlying protein surface, but also on the precise topography and chemical pattern of amino acids. Nevertheless, understanding the role of water in protein interactions is essential to understanding, predicting, and eventually controlling such interactions, which play a crucial role in the development of therapeutic strategies and in protein separations. In this presentation, I will discuss our recent efforts on quantitatively characterizing this disruption of water structure, with the goal of using this information for efficiently predicting protein interaction interfaces as well the design of ligands with high affinity and specificity.