Structural and thermodynamic analysis of factors governing the stability and thermal folding/unfolding of SazCA.

ABSTRACT: Molecular basis of protein stability at different temperatures is a fundamental problem in protein science that is substantially far from being accurately and quantitatively solved as it requires an explicit knowledge of the temperature dependence of folding free energy of amino acid residues. In the present study, we attempted to gain insights into the thermodynamic stability of SazCA and its implications on protein folding/unfolding. We report molecular dynamics simulations of water solvated SazCA in a temperature range of 293-393 K to study the relationship between the thermostability and flexibility. Our structural analysis shows that the protein maintains the highest structural stability at 353 K and the protein conformations are highly flexible at temperatures above 353 K. Larger exp

SUBMITTER: Kumar S 

PROVIDER: S-EPMC8049272 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature