Efficient Methods for Characterizing Biomolecular Hydration and Interactions

The hydrophobicity of a protein surface dictates its interactions with ligands, other proteins, and extended interfaces. However, the hydrophobicity of a complex, heterogeneous protein surface depends, not only on the chemistry of the underlying amino acids, but also on the precise chemical pattern and topographical context presented by the protein surface. Methods for accurately and efficiently determining the context-dependent hydrophobicity of protein surfaces will presented. Further, how such estimates of protein hydrophobicity can be used to estimate interactions between two such protein surfaces will be discussed. Finally, the use of this framework to determine protein interaction interfaces will be demonstrated.