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  Proton detected solid-state NMR of membrane proteins at 28 Tesla (1.2 GHz) and 100 kHz magic-angle spinning

Nimerovsky, E., Tekwani Movellan, K., Zhang, X. C., Forster, M. C., Najbauer, E., Xue, K., et al. (2021). Proton detected solid-state NMR of membrane proteins at 28 Tesla (1.2 GHz) and 100 kHz magic-angle spinning. Biomolecules, 11(5): 752. doi:10.3390/biom11050752.

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 Creators:
Nimerovsky, E.1, Author              
Tekwani Movellan, K.2, Author              
Zhang, X. C., Author
Forster, M. C., Author
Najbauer, E.2, Author              
Xue, K.2, Author              
Dervisoglu, R.2, Author              
Giller, K.3, Author              
Griesinger, C.4, Author              
Becker, S.4, Author              
Andreas, L. B.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
2Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              
3Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
4Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: magic-angle spinning; solid-state NMR; membrane protein; beta barrel; transmembrane; proton detection; high magnetic field
 Abstract: The available magnetic field strength for high resolution NMR in persistent superconducting magnets has recently improved from 23.5 to 28 Tesla, increasing the proton resonance frequency from 1 to 1.2 GHz. For magic-angle spinning (MAS) NMR, this is expected to improve resolution, provided the sample preparation results in homogeneous broadening. We compare two-dimensional (2D) proton detected MAS NMR spectra of four membrane proteins at 950 and 1200 MHz. We find a consistent improvement in resolution that scales superlinearly with the increase in magnetic field for three of the four examples. In 3D and 4D spectra, which are now routinely acquired, this improvement indicates the ability to resolve at least 2 and 2.5 times as many signals, respectively.

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Language(s): eng - English
 Dates: 2021-05-18
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.3390/biom11050752
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Title: Biomolecules
Source Genre: Journal
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Pages: - Volume / Issue: 11 (5) Sequence Number: 752 Start / End Page: - Identifier: -