Multi-mode water dynamics in hydration shells of villin headpiece subdomain protein in the solid state using deuterium and oxygen-17 NMR spectroscopy.

ABSTRACT: Hydration shell properties in proteins remain an active topic of investigation due to their complexity and importance for biological processes. We focused on hydration shell dynamics in the solid state of the globular villin headpiece subdomain (HP36). We utilized 2H (D2O hydration) and 17O (H217O hydration) solid-state NMR spectroscopy in combination with computational modeling to obtain a comprehensive picture of water motions, starting from high-amplitude modes such as diffusion and large-angle tetrahedral jumps and progressing to lower-amplitude modes such as 2-site deuteron flips and small-angle fluctuations. The measurements consisted of NMR line shapes as well as laboratory and rotating frame relaxation rates using novel approaches, conducted in the 300-170 K temperature range and a

SUBMITTER: Vugmeyster L 

PROVIDER: S-EPMC12398340 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature