Abstract
The SARS-CoV-2 main protease (Mpro) is a serine-type protease with catalytic residues His-41 and Cys-145. These residues cleave highly specific protein sequences, making Mpro a vital part of the viral replication process and an attractive target for inhibitor design. As the virus spreads across the globe, sequence mutations occur, creating an additional challenge for robust inhibitor design. In previous work we have reported results from sequence analysis, structure prediction, and molecular modeling of the first seventy-nine Mpro variants, which revealed patterns in residue substitutions and a distribution of cohesion and constraint in the active site due to mutations.
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