Ultrahigh Resolution in Proton Solid-State NMR Spectroscopy at High Levels of Deuteration

Slim peaks: Using a perdeuterated protein recrystallized from a 10:90 H2O:D2O mixture in magic‐angle spinning (MAS) solid‐state NMR spectroscopy experiments gives small 1H line widths at moderate spinning frequencies without application of homonuclear decoupling. This labeling strategy opens new per...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2006-06, Vol.45 (23), p.3878-3881
Main Authors: Chevelkov, Veniamin, Rehbein, Kristina, Diehl, Anne, Reif, Bernd
Format: Article
Language:English
Subjects:
Deuterium - chemistry
line widths
magic-angle spinning
Magnetic Resonance Spectroscopy
predeuteration
proteins
Protons
solid-state NMR spectroscopy
structure elucidation
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Summary:Slim peaks: Using a perdeuterated protein recrystallized from a 10:90 H2O:D2O mixture in magic‐angle spinning (MAS) solid‐state NMR spectroscopy experiments gives small 1H line widths at moderate spinning frequencies without application of homonuclear decoupling. This labeling strategy opens new perspectives for assignment of large protein spin systems.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200600328