Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca²⁺-ligated calmodulin.

ABSTRACT: Recent advances in rapid mixing and freeze quenching have opened the path for time-resolved electron paramagnetic resonance (EPR)-based double electron-electron resonance (DEER) and solid-state NMR of protein-substrate interactions. DEER, in conjunction with phase memory time filtering to quantitatively extract species populations, permits monitoring time-dependent probability distance distributions between pairs of spin labels, while solid-state NMR provides quantitative residue-specific information on the appearance of structural order and the development of intermolecular contacts between substrate and protein. Here, we demonstrate the power of these combined approaches to unravel the kinetic and structural pathways in the binding of the intrinsically disordered peptide substrate (M13)

SUBMITTER: Schmidt T 

PROVIDER: S-EPMC8833187 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature