| Autor: |
Díaz, Natalia, Suárez, Dimas |
| Předmět: |
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| Zdroj: |
Chemical Communications; 5/28/2021, Vol. 57 Issue 43, p5314-5317, 4p |
| Abstrakt: |
While the state-of-the-art computational simulations support the neutral state for the catalytic dyad of the SARS-CoV-2 main protease, the recently-reported neutron structure exhibits a zwitterionic form. To better compare the structural and dynamical features of the two charge configurations, we perform a Molecular Dynamics study of the dimeric enzyme in complex with a peptide substrate. The simulations show that the enzyme charge configuration from the neutron structure is not compatible with a catalytically-competent binding mode for peptide substrates. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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