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Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements

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Abstract

Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is a major technique for the characterization of the structural dynamics of biopolymers at atomic resolution. However, the intrinsic low sensitivity of this technique poses significant limitations to its routine application in structural biology. Here we achieve substantial savings in experimental time using a new subclass of Polarization Optimized Experiments (POEs) that concatenate TEDOR and SPECIFIC-CP transfers into a single pulse sequence. Specifically, we designed new 2D and 3D experiments (2D TEDOR-NCX, 3D TEDOR-NCOCX, and 3D TEDOR-NCACX) to obtain distance measurements and heteronuclear chemical shift correlations for resonance assignments using only one experiment. We successfully tested these experiments on N-Acetyl-Val-Leu dipeptide, microcrystalline U-13C,15N ubiquitin, and single- and multi-span membrane proteins reconstituted in lipid membranes. These pulse sequences can be implemented on any ssNMR spectrometer equipped with standard solid-state hardware using only one receiver. Since these new POEs speed up data acquisition considerably, we anticipate their broad application to fibrillar, microcrystalline, and membrane-bound proteins.

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Acknowledgements

This work was supported by the National Institute of Health (GM 64742 to G.V. and R35 GM118047 to H.A.). Many thanks to Dr. D. Weber for critical reading and editing the manuscript.

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  1. Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, 6-155 Jackson Hall, Minneapolis, MN, 55455, USA

    T. Gopinath, Songlin Wang, John Lee, Hideki Aihara & Gianluigi Veglia

  2. Department of Chemistry, University of Minnesota, Minneapolis, MN, 55455, USA

    Gianluigi Veglia

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  1. T. Gopinath
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Correspondence to Gianluigi Veglia.

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Gopinath, T., Wang, S., Lee, J. et al. Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements. J Biomol NMR 73, 141–153 (2019). https://doi.org/10.1007/s10858-019-00237-5

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