NMR-detected brownian dynamics of αB-crystallin over a wide range of concentrations.

ABSTRACT: Knowledge about the global translational and rotational motion of proteins under crowded conditions is highly relevant for understanding the function of proteins in vivo. This holds in particular for human αB-crystallin, which is strongly crowded in vivo and inter alia responsible for preventing cataracts. Quantitative information on translational and rotational diffusion is not readily available, and we here demonstrate an approach that combines pulsed-field-gradient NMR for translational diffusion and proton T1ρ/T2 relaxation-time measurements for rotational diffusion, thus overcoming obstacles encountered in previous studies. The relaxation times measured at variable temperature provide a quantitative measure of the correlation function of protein tumbling, which cannot be approximated

SUBMITTER: Roos M 

PROVIDER: S-EPMC4286604 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature