Influence of the solvent structure on the electrostatic interactions in proteins.

The proper estimation of the influence of the many-body dynamic solvent microstructure on a pairwise electrostatic interaction (PEI) at the protein-solvent interface is very important for solving many biophysical problems. In this work, the PEI energy was calculated for a system that models the interface between a protein and an aqueous solvent. The concept of nonlocal electrostatics for interfacial electrochemical systems was used to evaluate the contribution of a solvent orientational polarization, correlated by the network of hydrogen bonds, into the PEI energy in proteins. The analytical expression for this energy was obtained in the form of Coulomb's law with an effective distance-dependent dielectric function. The asymptotic and numerical analysis carried out for this function revealed several features of dielectric heterogeneity at the protein-solvent interface. For charges located in close proximity to this interface, the values of the dielectric function for the short-distance electrostatic interactions were found to be remarkably smaller than those determined by the classical model, in which the solvent was considered as the uniform dielectric medium of high dielectric constant. Our results have shown that taking into consideration the dynamic solvent microstructure remarkably increases the value of the PEI energy at the protein-solvent interface.