Abstract
Amyloids are a class of noncrystalline, yet ordered, protein aggregates. A new approach was used to provide the initial structural data on an amyloid fibril—comprising a peptide (β34–42) from the C-terminus of the β-amyloid protein—based on measurement of intramolecular 13C–13C distances and 13C chemical shifts by solid-state 13C NMR and individual amide absorption frequencies by isotope-edited infrared spectroscopy. Intermolecular orientation and alignment within the amyloid sheet was determined by fitting models to observed intermolecular 13C–13C couplings. Although the structural model we present is defined to relatively low resolution, it nevertheless shows a pleated antiparallel β-sheet characterized by a specific intermolecular alignment.
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Lansbury, P., Costa, P., Griffiths, J. et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Mol Biol 2, 990–998 (1995). https://doi.org/10.1038/nsb1195-990
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DOI: https://doi.org/10.1038/nsb1195-990
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