Mathematical simulation of interactions of protein molecules and prediction of their reactivity

Abstract

A physical model of interactions of protein molecules has been developed. The regularities of their reactivity have been studied using electrostatics methods for two histone dimers H2A–H2B and H3–H4 assembled from monomers. The formation of histone dimers from different monomers has been simulated and their ability to the formation of stable compounds has been investigated by analyzing the potential energy matrix using the condition number. The results of a simulation of the electrostatic interaction in the formation of dimers from complete amino acid sequences of selected proteins and their truncated analogs have been considered. The calculations have been performed taking into account the screening of the electrostatic charge of charged amino acids for different concentrations of the monovalent salt using the Gouy–Chapman theory.