Accurate determination of 1H‐15N dipolar couplings using inaccurate settings of 
the magic angle in solid‐state NMR spectroscopy.

Xue, K.; Mühlbauer, M.; Mamone, S.; Sarkar, R.; Reif, B.

doi:10.1002/anie.201814314

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Journal Article

Accurate determination of ¹H‐¹⁵N dipolar couplings using inaccurate settings of the magic angle in solid‐state NMR spectroscopy.

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Mamone, S.
Research Group of NMR Signal Enhancement, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Xue, K., Mühlbauer, M., Mamone, S., Sarkar, R., & Reif, B. (2019). Accurate determination of ¹H‐¹⁵N dipolar couplings using inaccurate settings of the magic angle in solid‐state NMR spectroscopy. Angewandte Chemie International Edition, 58(13), 4286-4290. doi:10.1002/anie.201814314.

Cite as: https://hdl.handle.net/21.11116/0000-0003-63D3-F

Abstract

Magic-angle spinning (MAS) is an essential ingredient in a wide variety of solid-state NMR experiments. The standard procedures to adjust the rotor angle are not highly accurate, resulting in a slight misadjustment of the rotor from the magic angle (RL= ) on the order of a few millidegrees. This small missetting has no significant impact on the overall spectral resolution, but is sufficient to reintroduce anisotropic interactions. Shown here is that site-specific H-1-N-15 dipolar couplings can be accurately measured in a heavily deuterated protein. This method can be applied at arbitrarily high MAS frequencies, since neither rotor synchronization nor particularly high radiofrequency field strengths are required. The off-MAS method allows the quantification of order parameters for very dynamic residues, which often escape an analysis using existing methods.