Connecting Protein Millisecond Conformational Dynamics to Protein Thermal Stability.

ABSTRACT: The stability of protein folded states is crucial for its function, yet the relationship with the protein sequence remains poorly understood. Prior studies have focused on the amino acid composition and thermodynamic couplings within a single folded conformation, overlooking the potential contribution of protein dynamics. Here, we address this gap by systematically analyzing the impact of alanine mutations in the C-terminal β-strand (β5) of ubiquitin, a model protein exhibiting millisecond timescale interconversion between two conformational states differing in the β5 position. Our findings unveil a negative correlation between millisecond dynamics and thermal stability, with alanine substitutions at seemingly flexible C-terminal residues significantly enhancing thermostability. Integratin

SUBMITTER: Hou XN 

PROVIDER: S-EPMC11350723 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature