Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph
Abstract
The formation of fibrils of the amyloid-β (Aβ) peptide is considered to be a key event in the pathology of Alzheimer’s disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular basis of AD. In this work, we present the sequential resonance assignment of one of the polymorphs of Aβ(1–42) fibrils. We show that most of the protein is rigid, while a stretch of 4 residues (11–14) is not visible by solid-state NMR spectroscopy due to dynamics. Mehr anzeigen
Persistenter Link
https://doi.org/10.3929/ethz-b-000116631Publikationsstatus
publishedExterne Links
Zeitschrift / Serie
Biomolecular NMR AssignmentsBand
Seiten / Artikelnummer
Verlag
SpringerThema
Alzheimer’s disease; Amyloid-β peptide; Amyloid fibrils; Solid-state NMR spectroscopyOrganisationseinheit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
03782 - Riek, Roland / Riek, Roland
Förderung
146757 - NMR studies in the Solid State (SNF)
159707 - NMR studies in the Solid State (SNF)
Anmerkungen
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.