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Linser, R.* ; Fink, U.* ; Reif, B.*

Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state.

J. Biomol. NMR 47, 1-6 (2010)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14-17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution demonstrates that MAS solid-state NMR on extensively deuterated proteins is able to compete with solution-state NMR spectroscopy if proteins are investigated with correlation times tau(c) that exceed 25 ns.
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Publication type Article: Journal article
Document type Scientific Article
Language english
Publication Year 2010
HGF-reported in Year 0
ISSN (print) / ISBN 0925-2738
e-ISSN 1573-5001
Quellenangaben Volume: 47, Issue: 1, Pages: 1-6 Article Number: , Supplement: ,
Publisher Springer
Reviewing status Peer reviewed
PubMed ID 20232230
Erfassungsdatum 2010-12-31