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• W4236801721 endingPage "4334" @default.
• W4236801721 startingPage "4330" @default.
• W4236801721 abstract "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 ( ) 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 1 H‐ 15 N 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." @default.
• W4236801721 created "2022-05-12" @default.
• W4236801721 creator A5034990314 @default.
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• W4236801721 date "2019-02-27" @default.
• W4236801721 modified "2023-10-16" @default.
• W4236801721 title "Accurate Determination of ¹ H‐ ¹⁵ N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy" @default.
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• W4236801721 doi "https://doi.org/10.1002/ange.201814314" @default.
• W4236801721 hasPublicationYear "2019" @default.
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