We seek to understand how Nature uses electrostatics in protein binding. Though electrostatics are but one component of the total binding free energy of protein complexes, electrostatics are commonly manipulated in design and are extremely relevant to protein recognition. This project aims to map out electrostatic contributions to protein-protein binding as they relate to structural components of proteins.  Using a continuum electrostatics model on a large set of protein complexes, we aim to quantify the electrostatic contributions of protein structural elements, such as backbone, side chain, proximal, and distal residues toward the binding free energy.  Particular questions this study addresses include whether protein specificity and promiscuity correlate to electrostatic component contribution and whether trends exist among proteins when correlated to monopole, fold, or size. By using a large number of protein structures, statistically significant trends may be elucidated.

Investigating the structural determinants of electrostatic binding among protein-protein complexes: A systematic, large-scale computational study

243rd National Meeting (2012)

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