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Journal Article

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


Andreas,  L. B.
Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society;

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Schubeis, T., Le Marchand, T., Andreas, L. B., & Pintacuda, G. (2018). 1H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins. Journal of Magnetic Resonance, 287, 140-152. doi:10.1016/j.jmr.2017.11.014.

Cite as: http://hdl.handle.net/21.11116/0000-0000-705D-A
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 1H-1H dipolar couplings, so that direct detection of the larger magnetic moment available from 1H 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 ten-fold 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 1H 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.