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

Peng Xiao, David Bolton, Rachel A. Munro, Leonid S. Brown () and Vladimir Ladizhansky ()
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Peng Xiao: University of Guelph
David Bolton: University of Guelph
Rachel A. Munro: University of Guelph
Leonid S. Brown: University of Guelph
Vladimir Ladizhansky: University of Guelph

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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 visualized through SSNMR-detected snapshots of H/D exchange patterns as a function of temperature, revealing the unfolding intermediate and its stabilizing factors. Our approach is transferable to other membrane proteins, and opens additional ways to characterize their unfolding and stabilizing interactions with atomic resolution.

Date: 2019
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DOI: 10.1038/s41467-019-11849-8

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