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Effect of Bovine Serum Albumin Redox Status on Its Interaction with Paraoxon as Determined by Molecular Modeling

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Fig. 1.

Abbreviations

OP:

organophosphate

BSA:

bovine serum albumin

HSA:

human serum albumin

MM-PBSA:

Molecular Mechanics–Poisson–Boltzmann Surface Area (an approach to estimate the binding free energy of small ligands to biological macromolecules)

distP-O:

the distance between the paraoxon phosphorous atom and the Tyr149 or Tyr410 hydroxyl oxygen atom

REFERENCES

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  2. Belinskaya, D.A., Taborskaya, K.I., Goncha-rov, N.V., Shmurak, V.I., Avdonin, P.P., and Avdonin, P.V., In silico analysis of paraoxon binding by human and bovine serum albumin, J. Evol. Biochem. Physiol., 2017, vol. 53(3), pp. 191–199.

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  6. Goncharov, N.V., Terpilovskii, M.A., Belinskaya, D.A., Shmurak, V.I., and Avdonin, P.V., Comparative analysis of esterase and paraoxonase activities of different serum albumin species, J. Evol. Biochem. Physiol., 2017, vol. 53(4), pp. 271–281.

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Funding

This work was implemented within the state assignment no. AAAA-А18-118012290142-9 and supported by the Russian Foundation for Basic Research (project no. 19-34-90026).

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Authors and Affiliations

  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg, Russia

    D. A. Belinskaia, A. A. Batalova & N. V. Goncharov

  2. Research Institute of Hygiene, Occupational Pathology and Human Ecology, St. Petersburg, Russia

    N. V. Goncharov

Authors
  1. D. A. Belinskaia
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  2. A. A. Batalova
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  3. N. V. Goncharov
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Corresponding author

Correspondence to D. A. Belinskaia.

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The present study involved neither human nor animal subjects as research objects.

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Belinskaia, D.A., Batalova, A.A. & Goncharov, N.V. Effect of Bovine Serum Albumin Redox Status on Its Interaction with Paraoxon as Determined by Molecular Modeling. J Evol Biochem Phys 56, 434–438 (2020). https://doi.org/10.1134/S0022093020050063

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