Understanding the role of water on temperature-dependent structural modifications of SARS CoV-2 main protease binding sites.

ABSTRACT: Thermally stable and labile proteases are found in microorganisms. Protease mediates the cleavage of polyproteins in the virus replication and transcription process. 6 µs MD simulations were performed for monomer/dimer SARS CoV-2 main protease system in both SPC/E and mTIP3P water model to analyse the temperature-dependent behaviour of the protein. It is found that maximum conformational changes are observed at 348 K which is near the melting temperature. Network distribution of evolved conformations shows an increase in the number of communities with the rise in the temperature. The global conformation of the protein was found to be intact whereas a local conformational space evolved due to thermal fluctuations. The global conformational change in the free energy ΔΔG value for the monomer

SUBMITTER: Venugopal PP 

PROVIDER: S-EPMC9297661 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature