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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)
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
ISSN (print) / ISBN
1433-7851
e-ISSN
1521-3773
Quellenangaben
Volume: 58,
Issue: 13,
Pages: 4286-4290
Publisher
Wiley
Publishing Place
Weinheim
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)