Abstract
The dynamics and thermodynamics of the homodimer main protease protein SARS-CoV-2 are analysed at the level of Elastic Network Models (ENM). Correlated motions display a rich and heterogeneous dynamical structure, including allosterically correlated motions between the active sites in the two domains. Exhaustive 1-point and 2-point mutation maps, and their effect on binding free energies and allosteric free energies confirm the susceptibility identified in recent candidate inhibitor assays, but also suggest several new candidate regions for control and inhibition of the protease function, which may assist the development of current fragment binding screens.
Competing Interest Statement
The authors have declared no competing interest.
Copyright
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