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

Angew. Chem.-Int. Edit. 58, 4286-4290 (2019)
Postprint online available 03/2020 Open Access Green as soon as is submitted to ZB.
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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Analytical Methods ; Nmr Spectroscopy ; Proteins ; Solid-state Experiments ; Structure Elucidation; Nuclear-magnetic-resonance; Mas Nmr; Proteins; Spectra; Resolution
Reviewing status