1 H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins

Tobias Schubeis (1) , Tanguy Le Marchand (1) , Loren B Andreas (2) , Guido Pintacuda (1)

1 Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie
2 MPI-BPC - Max Planck Institute for Biophysical Chemistry

Building on a decade of continuous advances of the community, the recent development of very fast (60 kHz and above) magic-angle spinning (MAS) probes has revolutionised the field of solid-state NMR. This new spinning regime reduces the 1 H-1 H dipolar couplings, so that direct detection of the larger magnetic moment available from 1 H is now possible at high resolution, not only in deuterated molecules but also in fully-protonated substrates. Such capabilities allow rapid " fingerprinting " of samples with a tenfold reduction of the required sample amounts with respect to conventional approaches, and permit extensive, robust and expeditious assignment of small-to-medium sized proteins (up to ca. 300 residues), and the determination of inter-nuclear proximities, relative orientations of secondary structural elements, protein-cofactor interactions, local and global dynamics. Fast MAS and 1 H detection techniques have nowadays been shown to be applicable to membrane-bound systems. This paper reviews the strategies underlying this recent leap forward in sensitivity and resolution, describing its potential for the detailed characterization of membrane proteins. Graphical TOC

Domaines: Chimie analytique

Tobias Schubeis, Tanguy Le Marchand, Loren B Andreas, Guido Pintacuda. 1 H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins. Journal of Magnetic Resonance, 2018, 287, pp.140-152. ⟨10.1016/j.jmr.2017.11.014⟩. ⟨hal-01744878⟩