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Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state

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Abstract

HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14–17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution demonstrates that MAS solid-state NMR on extensively deuterated proteins is able to compete with solution-state NMR spectroscopy if proteins are investigated with correlation times τ c that exceed 25 ns.

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Acknowledgments

We thank Peter Schmieder for continuous support. This research was supported by the Leibniz-Gemeinschaft (WGL) and the DFG (Re1435, SFB449, SFB740, FOR475). R. L. is a Kekulé scholar and acknowledges financial support by the Verband der Chemischen Industrie (VCI).

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Authors and Affiliations

  1. Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle Str. 10, 13125, Berlin, Germany

    Rasmus Linser, Uwe Fink & Bernd Reif

  2. Charité Universitätsmedizin, 10115, Berlin, Germany

    Bernd Reif

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  1. Rasmus Linser
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  2. Uwe Fink
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  3. Bernd Reif
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Correspondence to Bernd Reif.

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Linser, R., Fink, U. & Reif, B. Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state. J Biomol NMR 47, 1–6 (2010). https://doi.org/10.1007/s10858-010-9404-1

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