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

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 DOI PMC
Open Access Green
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter 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
Zeitschrift Angewandte Chemie - Internationale Edition
Quellenangaben Band: 58, Heft: 13, Seiten: 4286-4290 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)