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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
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
Zeitschrift
Angewandte Chemie - Internationale Edition
Quellenangaben
Band: 51,
Heft: 25,
Seiten: 6136-6139
Verlag
Wiley
Verlagsort
Weinheim
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)