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.
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Acknowledgments
This work was supported by grants from Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (200020_146757 and 200020_159707) and the ETH Zürich Research Commission TH 16 09-3 to BHM and by Grants ANR-12-BS08-0013-01 and ANR-14-CE09-0024B from the Agence Nationale de la Recherche to AB.
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Francesco Ravotti and Marielle Aulikki Wälti contributed equally.
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Ravotti, F., Wälti, M.A., Güntert, P. et al. Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph. Biomol NMR Assign 10, 269–276 (2016). https://doi.org/10.1007/s12104-016-9682-y
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DOI: https://doi.org/10.1007/s12104-016-9682-y