Analysis of Ten Microsecond simulation data of SARS-CoV-2 dimeric main protease

Abstract

The dimeric main protease of SARS-CoV-2, has become a crucial target for inhibiting/modulating its catalytic activity. However, understanding of its conformational change, and atomistic flexibility, is very much lucrative for designing/developing small molecules. Fortunately, huge data has been revealed by a research group, performed about ten-microsecond molecular dynamics to paving the way for understanding the structural complexity of protease. Herein, we have done the basic structural analysis, advanced flexibility and conformational analysis like PCA, for revealing out the regions and residues, which are mostly flexible and likely to be responsible for different conformation of protease protein.