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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Veröffentlicht in:	Angewandte Chemie International Edition 2006-06, Vol.45 (23), p.3878-3881
Hauptverfasser:	Chevelkov, Veniamin, Rehbein, Kristina, Diehl, Anne, Reif, Bernd
Format:	Artikel
Sprache:	eng
Schlagworte:	Deuterium - chemistry line widths magic-angle spinning Magnetic Resonance Spectroscopy predeuteration proteins Protons solid-state NMR spectroscopy structure elucidation
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Zusammenfassung:	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