Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.

ABSTRACT: Membrane protein folding, structure, and function strongly depend on a cell membrane environment, yet detailed characterization of folding within a lipid bilayer is challenging. Studies of reversible unfolding yield valuable information on the energetics of folding and on the hierarchy of interactions contributing to protein stability. Here, we devise a methodology that combines hydrogen-deuterium (H/D) exchange and solid-state NMR (SSNMR) to follow membrane protein unfolding in lipid membranes at atomic resolution through detecting changes in the protein water-accessible surface, and concurrently monitoring the reversibility of unfolding. We obtain atomistic description of the reversible part of a thermally induced unfolding pathway of a seven-helical photoreceptor. The pathway is visuali

SUBMITTER: Xiao P 

PROVIDER: S-EPMC6711998 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature