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.

doi:10.1007/s10858-015-9902-2

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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;

/persons/resource/persons36496

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

/persons/resource/persons14824

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

/persons/resource/persons15414

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

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http://link.springer.com/content/pdf/10.1007%2Fs10858-015-9902-2.pdf
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引用

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.

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

要旨

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.