This Article Full Text Full Text (PDF) Figures Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Sulea, T. Articles by Purisima, E. O. Search for Related Content PubMed PubMed Citation Articles by Sulea, T. Articles by Purisima, E. O.

Profiling Charge Complementarity and Selectivity for Binding at the Protein Surface

Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H4P 2R2, Canada

Correspondence: Address reprint requests to E. O. Purisima, E-mail: enrico.purisima{at}nrc.ca.

A novel analysis and representation of the protein surface in terms of electrostatic binding complementarity and selectivity is presented. The charge optimization methodology is applied in a probe-based approach that simulates the binding process to the target protein. The molecular surface is color coded according to calculated optimal charge or according to charge selectivity, i.e., the binding cost of deviating from the optimal charge. The optimal charge profile depends on both the protein shape and charge distribution whereas the charge selectivity profile depends only on protein shape. High selectivity is concentrated in well-shaped concave pockets, whereas solvent-exposed convex regions are not charge selective. This suggests the synergy of charge and shape selectivity hot spots toward molecular selection and recognition, as well as the asymmetry of charge selectivity at the binding interface of biomolecular systems. The charge complementarity and selectivity profiles map relevant electrostatic properties in a readily interpretable way and encode information that is quite different from that visualized in the standard electrostatic potential map of unbound proteins.