Abstract
We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically optimised symmetry-based mixing sequences and the simultaneous recording of chemical shift correlation spectra such as: 3D NCAC and 3D NHH with dual receivers, 3D NC′C and 3D C′NCA with sequential 13C acquisitions, 3D NHH and 3D NC′H with sequential 1H acquisitions and 3D CANH and 3D C’NH with broadband 13C–15N mixing are demonstrated using microcrystalline samples of the β1 immunoglobulin binding domain of protein G (GB1) and the chicken α-spectrin SH3 domain.
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Acknowledgments
The FLI is a member of the Science Association’Gottfried Wilhelm Leibniz’ (WGL) and is financially supported by the Federal Government of Germany and the State of Thuringia. Also thanks to the Leibniz Graduate School on Aging and Age-Related Diseases (LGSA) for funding and support.
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Bellstedt, P., Herbst, C., Häfner, S. et al. Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra. J Biomol NMR 54, 325–335 (2012). https://doi.org/10.1007/s10858-012-9680-z
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DOI: https://doi.org/10.1007/s10858-012-9680-z