Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 10, Issue 2, Pages 269-276Publisher
SPRINGER
DOI: 10.1007/s12104-016-9682-y
Keywords
Alzheimer's disease; Amyloid-beta peptide; Amyloid fibrils; Solid-state NMR spectroscopy
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Funding
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung [200020_146757, 200020_159707]
- ETH Zurich Research Commission [TH 16 09-3]
- Agence Nationale de la Recherche [ANR-12-BS08-0013-01, ANR-14-CE09-0024B]
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The formation of fibrils of the amyloid-beta (A beta) 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 A beta(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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