Structural stability of the SARS-CoV-2 main protease: Can metal ions affect function?

ABSTRACT: We have investigated the structural stability of the SARS (Severe acute respiratory syndrome)-CoV-2 main protease monomer (Mpro). We quantified the spatial and angular changes in the structure using two independent analyses, one based on a spatial metrics (δ, ratio), the second on angular metrics. The order of unfolding of the 10 helices in Mpro is characterized by beta vs alpha plots similar to those of cytochromes and globins. The longest turning region is anomalous in the earliest stage of unfolding. In an investigation of excluded-volume effects, we found that the maximum spread in average molecular-volume values for Mpro, cytochrome c-b₅₆₂, cytochrome c', myoglobin, and cytoglobin is ~10 Å³. This apparent universality is a consequence of the dominant contribution

SUBMITTER: Kozak JJ 

PROVIDER: S-EPMC7365078 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature