Open Access Green as soon as Postprint is submitted to ZB.
Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state.
J. Biomol. NMR 47, 1-6 (2010)
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.
Impact Factor
Scopus SNIP
Scopus
Cited By
Cited By
Altmetric
0.000
1.170
28
Annotations
Special Publikation
Hide on homepage
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
Journal
Journal of Biomolecular NMR
Quellenangaben
Volume: 47,
Issue: 1,
Pages: 1-6
Publisher
Springer
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
PubMed ID
20232230
Erfassungsdatum
2010-12-31