Conformational entropy of a single peptide controlled under force governs protease recognition and catalysis.

ABSTRACT: An immense repertoire of protein chemical modifications catalyzed by enzymes is available as proteomics data. Quantifying the impact of the conformational dynamics of the modified peptide remains challenging to understand the decisive kinetics and amino acid sequence specificity of these enzymatic reactions in vivo, because the target peptide must be disordered to accommodate the specific enzyme-binding site. Here, we were able to control the conformation of a single-molecule peptide chain by applying mechanical force to activate and monitor its specific cleavage by a model protease. We found that the conformational entropy impacts the reaction in two distinct ways. First, the flexibility and accessibility of the substrate peptide greatly increase upon mechanical unfolding. Second, the con

SUBMITTER: Guerin ME 

PROVIDER: S-EPMC6233122 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature