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

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.

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Schubeis, T., Author
Le Marchand, T., Author
Andreas, L. B.1, Author           
Pintacuda, G., Author
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1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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Free keywords: Fast MAS; 1H detection; Resolution; Sensitivity; Deuteration; Membrane proteins
 Abstract: 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.

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Language(s): eng - English
 Dates: 2018-02-052018-02
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmr.2017.11.014
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Title: Journal of Magnetic Resonance
Source Genre: Journal
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Pages: - Volume / Issue: 287 Sequence Number: - Start / End Page: 140 - 152 Identifier: -