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Open Access Green as soon as Postprint is submitted to ZB.
Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure.
Phys. Chem. Chem. Phys. 15, 12551-12557 (2013)
The amyloid beta-peptide (A beta) is the major structural component of amyloid fibrils in the plaques of brains of Alzheimer's disease patients. Numerous studies have addressed important aspects of secondary and tertiary structure of fibrils. In electron microscopic images, fibrils often bundle together. The mechanisms which drive the association of protofilaments into bundles of fibrils are not known. We show here that amino acid side chain exchangeable groups like e. g. histidines can provide useful restraints to determine the quarternary assembly of an amyloid fibril. Exchangeable protons are only observable if a side chain hydrogen bond is formed and the respective protons are protected from exchange. The method relies on deuteration of the A beta peptide. Exchangeable deuterons are substituted with protons, before fibril formation is initiated.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Solid-state Nmr ; Perdeuterated Proteins ; Alzheimers-disease ; Correlation Spectroscopy ; Experimental Constraints ; Membrane-proteins ; Beta-protein ; Fibrils ; Resolution ; A-beta(1-40)
ISSN (print) / ISBN
0956-5000
e-ISSN
1364-5455
Quellenangaben
Volume: 15,
Issue: 30,
Pages: 12551-12557
Publisher
Royal Society of Chemistry (RSC)
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)