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Efficient band-selective homonuclear CO–CA cross-polarization in protonated proteins

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Abstract

Previously introduced for highly deuterated proteins, band-selective magnetization transfer between CO and CA spins by dipolar-based homonuclear cross polarization is applied here to a protonated protein. Robust and efficient recoupling is achieved when the sum of effective radio-frequency fields on CO and CA resonances equals two times the spinning rate, yielding up to 33 % of magnetization transfer efficiency in protonated ubiquitin. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields when the isotropic chemical shift difference of CO and CA considerably exceeds the spinning rate. This method has been implemented in NiCOi−1CAi−1 and CAi(Ni)COi−1CAi−1 two-dimensional interresidual correlation experiments for fast and efficient resonance assignment of ubiquitin by solid-state NMR spectroscopy.

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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.

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Authors and Affiliations

  1. Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

    Veniamin Chevelkov, Chaowei Shi, Hannes Klaus Fasshuber, Stefan Becker & Adam Lange

  2. School of Life Sciences, University of Science and Technology of China, Hefei, China

    Chaowei Shi

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  1. Veniamin Chevelkov
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  2. Chaowei Shi
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  3. Hannes Klaus Fasshuber
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  4. Stefan Becker
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  5. Adam Lange
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Correspondence to Adam Lange.

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Chevelkov, V., Shi, C., Fasshuber, H.K. et al. Efficient band-selective homonuclear CO–CA cross-polarization in protonated proteins. J Biomol NMR 56, 303–311 (2013). https://doi.org/10.1007/s10858-013-9767-1

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