A new method, which analyzes the potential energy of electrostatic interaction of protein complexes at point replacements of amino acid residues assuming a three-dimensional structure of the complex on the example of formation of a Nap1–Nap1 dimer, has been presented. Maps of potential energy of electrostatic interaction of paired amino acid residues of participating proteins have been developed.
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The authors declare that they do not have any conflicts of interest.
Translated by A. Muravev
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Koshlan, T.V., Kulikov, K.G. Analysis of Electrostatic Interactions of Amino Acid Residues by the Example of Formation of a Nap1–Nap1 Dimer. Tech. Phys. 65, 333–339 (2020). https://doi.org/10.1134/S1063784220030123