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

Journal of Biomolecular NMR volume 61, pages 151–160 (2015)Cite this article

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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Acknowledgments

We thank Brigitta Angerstein for expert technical assistance. This work was supported by the Max Planck Society, the Leibniz-Gemeinschaft, and the DFG (Emmy Noether Fellowship to A.L). A.L. and S.X. acknowledge funding from the CRC803 (DFG).

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Authors and Affiliations

  1. Max-Planck-Institut für biophysikalische Chemie (MPI-bpc), Am Fassberg 11, 37077, Goettingen, Germany

    Veniamin Chevelkov, ShengQi Xiang, Karin Giller, Stefan Becker & Adam Lange

  2. Leibnizinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Str. 10, 13125, Berlin, Germany

    Veniamin Chevelkov & Adam Lange

  3. Institut für Biologie, Humboldt Universität zu Berlin, Invalidenstr 110, 10115, Berlin, Germany

    Adam Lange

  4. Munich Center for Integrated Protein Science (CIPS-M), Department Chemie, Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany

    Bernd Reif

  5. Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt (HMGU), Ingolstädter Landstr. 1, 85764, Neuherberg, Germany

    Bernd Reif

Authors
  1. Veniamin Chevelkov
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  2. ShengQi Xiang
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  3. Karin Giller
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  4. Stefan Becker
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  5. Adam Lange
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  6. Bernd Reif
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Correspondence to Veniamin Chevelkov.

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Chevelkov, V., Xiang, S., Giller, K. et al. Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization. J Biomol NMR 61, 151–160 (2015). https://doi.org/10.1007/s10858-015-9902-2

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