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Journal Article

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

MPS-Authors
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Chevelkov,  V.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Giller,  K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lange,  A.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://link.springer.com/content/pdf/10.1007%2Fs10858-015-9902-2.pdf
(Publisher version)

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Supplementary Material (public)

2105137_Suppl_1.doc
(Supplementary material), 2MB

2105137_Suppl_2.pdf
(Supplementary material), 18KB

2105137_Suppl_3.pdf
(Supplementary material), 15KB

Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0025-05CA-B
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.