Using Surface Hydrophobicity Together with Empirical Potentials to Identify Protein-Protein Binding Sites: Application to the Interactions of E-cadherins.

Studying the interactions within protein structures can inform about the details of how proteins of various types interact and aggregate. Empirical contact potentials have proven to be extremely important in the evaluation of individual modeled protein structures, but have found few applications to protein-protein interactions. In part, this is caused by a lack of properly formulated potentials with a proper reference state. Since the comparisons are made between different bound structures, the proper reference state should take into account other contacts. Therefore, a preferred reference state should be defined with respect to a given residue type interacting with an average residue instead of interacting with solvent as typically is used in derivation of statistical contact potentials. Here, a two-stage procedure for generating and evaluating interacting protein pairs is described, and an example of E-cadherin interactions is shown.