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BSH-CP based 3D solid-state NMR experiments for protein resonance assignment

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Abstract

We have recently presented band-selective homonuclear cross-polarization (BSH-CP) as an efficient method for CO–CA transfer in deuterated as well as protonated solid proteins. Here we show how the BSH-CP CO–CA transfer block can be incorporated in a set of three-dimensional (3D) solid-state NMR (ssNMR) pulse schemes tailored for resonance assignment of proteins at high static magnetic fields and moderate magic-angle spinning rates. Due to the achieved excellent transfer efficiency of 33 % for BSH-CP, a complete set of 3D spectra needed for unambiguous resonance assignment could be rapidly recorded within 1 week for the model protein ubiquitin. Thus we expect that BSH-CP could replace the typically used CO–CA transfer schemes in well-established 3D ssNMR approaches for resonance assignment of solid biomolecules.

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Acknowledgments

We thank Karin Giller and Brigitta Angerstein for expert technical assistance. This work was supported by the Max Planck Society, the DFG (Emmy Noether Fellowship to A. L.), and the European Union Seventh Framework Program under Grant Agreement 261863 (Bio-NMR). C. S. acknowledges funding from the MPG-CAS Joint Doctoral Promotion Programme. B. H. acknowledges EMBO for a long-term postdoctoral fellowship.

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Authors and Affiliations

  1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany

    Chaowei Shi, Hannes K. Fasshuber, Veniamin Chevelkov, Shengqi Xiang, Birgit Habenstein, Suresh Kumar Vasa, Stefan Becker & Adam Lange

  2. School of Life Sciences, University of Science and Technology of China, 96 JinZhai Road, 230026, Hefei, People’s Republic of China

    Chaowei Shi

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  1. Chaowei Shi
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  2. Hannes K. Fasshuber
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  3. Veniamin Chevelkov
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  4. Shengqi Xiang
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  5. Birgit Habenstein
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  7. Stefan Becker
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  8. Adam Lange
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Correspondence to Adam Lange.

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Shi, C., Fasshuber, H.K., Chevelkov, V. et al. BSH-CP based 3D solid-state NMR experiments for protein resonance assignment. J Biomol NMR 59, 15–22 (2014). https://doi.org/10.1007/s10858-014-9820-8

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