Protein conformational dynamics studied by ¹⁵N and ¹H R_1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals.

ABSTRACT: Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45-60kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use ¹⁵N R_1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-^1</

SUBMITTER: Gauto DF 

PROVIDER: S-EPMC5531261 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature