Long range electromagnetic effects drive protein-protein approaches: an egg of Coulomb

Abstract

AbstractLiving systems cannot rely on random intermolecular approaches inside cell crowding and hidden mechanisms must be present to favor only those molecular interactions which are specifically required by biological functions. Electromagnetic messaging among proteins is here hypothesized upon the observation that charged amino acids are most commonly located in adjacent sequence positions and/or in spatial close proximity. Molecular Dynamics simulations have been used to explore possible effects arising from concerted motions of charged amino acid side chains in two protein model systems. Protein electrodynamics seems to emerge as the framework for understanding long distance protein-ligand interactions.HighlightsProtein surfaces are often occupied by nearby side chains bearing opposite charges;Coulomb interactions determine hindered reorientations of charged side chains;MD simulations suggest time scales and extents of surface charge interactions;concerted motions of electric charges can yield electromagnetic protein signaling.