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Analysis of Electrostatic Interactions of Amino Acid Residues by the Example of Formation of a Nap1–Nap1 Dimer

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Abstract

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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Authors and Affiliations

  1. St. Petersburg State University, 199034, St. Petersburg, Russia

    T. V. Koshlan

  2. Peter the Great St.Petersburg Polytechnical University, 195251, St. Petersburg, Russia

    K. G. Kulikov

Authors
  1. T. V. Koshlan
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  2. K. G. Kulikov
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Corresponding author

Correspondence to K. G. Kulikov.

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The authors declare that they do not have any conflicts of interest.

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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

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  • DOI: https://doi.org/10.1134/S1063784220030123

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