Expression, purification, and biophysical characterization of recombinant MERS-CoV main (M^pro) protease.

ABSTRACT: MERS-CoV main protease (M^pro) is essential for the maturation of the coronavirus; therefore, considered a potential drug target. Detailed conformational information is essential to developing antiviral therapeutics. However, the conformation of MERS-CoV M^pro under different conditions is poorly characterized. In this study, MERS-CoV M^pro was recombinantly produced in E.coli and characterized its structural stability with respect to changes in pH and temperatures. The intrinsic and extrinsic fluorescence measurements revealed that MERS-CoV M^pro tertiary structure was exposed to the polar environment due to the unfolding of the tertiary structure. However, the secondary structure of MERS-CoV M^pro was gained at low pH because of charge-ch

SUBMITTER: Almutairi GO 

PROVIDER: S-EPMC9017057 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature