Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.

ABSTRACT: Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude and time scales, and are often related to biological function. Whereas solid-state NMR (SSNMR) spectroscopy has recently been used to characterize conformational ensembles of proteins in the microcrystalline states, its applications to membrane proteins remain limited. Here we use SSNMR to study conformational dynamics of a seven-helical transmembrane (TM) protein, Anabaena Sensory Rhodopsin (ASR) reconstituted in lipids. We report on site-specific measurements of the ¹⁵N longitudinal R₁ and rotating frame R_1ρ relaxation rates at two fields of 600 and 800 MHz and at two temperatures of 7

SUBMITTER: Good D 

PROVIDER: S-EPMC5510093 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature