Mathematical modeling of the temperature effect on the character of linking between monomeric proteins in aqueous solutions

This work is devoted to the mathematical modeling of the temperature effect on the stability of H2A–H2B and Н3–H4 histone dimers by studying their behavior in different temperature regimes of 20–50$^\circ$C. The study of the thermal stability of these two dimers in aqueous solutions at different temperatures has revealed their multifarious behavior at temperatures at 20–50$^\circ$C. Analysis has shown that dimer Н3–H4 is prone to aggregation due to an increase in the force of linking between histones Н3 and H4. Studies of the behavior of histone dimer H2A–H2B have disclosed different temperature transitions in its structure with a maximum peak at a temperature 45$^\circ$C.