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Zanetti_etal.pdf (6.03 MB)

Tuning Proton Transfer Thermodynamics in SARS-Cov-2 Main Protease: Implications for Catalysis and Inhibitor Design

preprint
submitted on 06.11.2020, 11:21 and posted on 06.11.2020, 13:21 by Laura Zanetti-Polzi, Micholas Smith, Chris Chipot, James C. Gumbart, Diane L. Lynch, Anna Pavlova, Jeremy C. Smith, Isabella Daidone
In this comutational work a hybrid quantum mechanics/molecular mechanics approach, the MD-PMM approach, is used to investigate the proton transfer reaction the activates the catalytic activity of SARS-CoV-2 main protease. The proton transfer thermodynamics is investigated for the apo ensyme (i.e., without any bound substrate or inhibitor) and in the presence of a inhibitor, N3, which was previously shown to covalently bind SARS-CoV-2 main protease.

History

Email Address of Submitting Author

laura.zanettipolzi@nano.cnr.it

Institution

Center S3, CNR Institute of Nanoscience

Country

Italy

ORCID For Submitting Author

0000-0002-2550-4796

Declaration of Conflict of Interest

No conflict of interest to declare

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