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  Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

Chevelkov, V., Xiang, S., Giller, K., Becker, S., Lange, A., & Reif, B. (2015). Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization. Journal of Biomolecular NMR, 61(2), 151-160. doi:10.1007/s10858-015-9902-2.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-05CA-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-09EA-B
Genre: Journal Article

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 Creators:
Chevelkov, V.1, Author              
Xiang, S., Author
Giller, K.2, Author              
Becker, S.2, Author              
Lange, A.1, Author              
Reif, B., Author
Affiliations:
1Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_persistent35              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: In this work, we show how the water flip-back approach that is widely employed in solution-state NMR can be adapted to proton-detected MAS solid-state NMR of highly deuterated proteins. The scheme allows to enhance the sensitivity of the experiment by decreasing the recovery time of the proton longitudinal magnetization. The method relies on polarization transfer from non-saturated water to the protein during the inter-scan delay.

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Language(s): eng - English
 Dates: 2015-01-302015-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-015-9902-2
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 61 (2) Sequence Number: - Start / End Page: 151 - 160 Identifier: -