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Open Access Green as soon as Postprint is submitted to ZB.
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
Angew. Chem.-Int. Edit. 51, 6136-6139 (2012)
Two-faced culprit: Fibrils of recombinantly produced amyloid β peptides (Aβs; residues 1–40) gave well-resolved solid-state NMR spectra. Two sets of resonances corresponding to residues 12–40 and 21–38 of the Aβ primary sequence were observed (see picture). Statistical analysis of electron microscopy data revealed that it was composed of a single Aβ polymorph, thus indicating that this Aβ fibril is composed of an asymmetric dimer.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Alzheimer's Disease; Amyloid Ss Peptides; Fibrillar Aggregates; Nmr Spectroscopy; Structural Biology; SOLID-STATE NMR; ANGLE-SPINNING NMR; EXPERIMENTAL CONSTRAINTS; STRUCTURAL MODEL; SPECTROSCOPY; POLYMORPHISM; PEPTIDE; PROTEIN; IDENTIFICATION; A-BETA(1-40)
ISSN (print) / ISBN
1433-7851
e-ISSN
1521-3773
Quellenangaben
Volume: 51,
Issue: 25,
Pages: 6136-6139
Publisher
Wiley
Publishing Place
Weinheim
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)