Coulomb energies of protein-protein complexes with monopole-free charge distributions

Abstract

From an analysis of Coulomb energy distributions of a large set of protein-protein complexes we show that the positive tail in the energy distribution disappears when the monopole-monopole term, the only energy term independent of inter-subunit orientations, is removed. This indicates that unfavorable Coulomb energies associated with subunit orientations are excluded in protein-protein complexes. The overall result remained unchanged when solvent effects were included. Our results have important bearing on the restriction of subunit orientations in protein-protein complexes and complement a recent work [K. Brock, K. Talley, K. Coley, P. Kundrotas, E. Alexov, Optimization of electrostatic interactions in protein-protein complexes, Biophys. J. 93 (2007) 3340-3352.] which showed that Coulomb energy of interaction in protein-protein complexes is sequence-optimized.