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Angew. Chem.-Int. Edit. 50, 4508-4512 (2011)
Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Publication type Article: Journal article
Document type Scientific Article
Keywords amyloid fibrils; lipid membrane; membrane proteins; outer membrane protein G; solid-state NMR spectroscopy
ISSN (print) / ISBN 1433-7851
Quellenangaben Volume: 50, Issue: 19, Pages: 4508-4512
Publishing Place Weinheim
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)