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J Mol Biol. 2012 Oct 26;423(3):454-61. doi: 10.1016/j.jmb.2012.08.004. Epub 2012 Aug 16.

Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.

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1
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235-1634, USA.

Abstract

Amyloid β protein (Aβ), the principal component of the extracellular plaques found in the brains of patients with Alzheimer's disease, forms fibrils well suited to structural study by X-ray fiber diffraction. Fiber diffraction patterns from the 40-residue form Aβ(1-40) confirm a number of features of a 3-fold symmetric Aβ model from solid-state NMR (ssNMR) but suggest that the fibrils have a hollow core not present in the original ssNMR models. Diffraction patterns calculated from a revised 3-fold hollow model with a more regular β-sheet structure are in much better agreement with the observed diffraction data than patterns calculated from the original ssNMR model. Refinement of a hollow-core model against ssNMR data led to a revised ssNMR model, similar to the fiber diffraction model.

PMID:
22903058
PMCID:
PMC3462308
DOI:
10.1016/j.jmb.2012.08.004
[Indexed for MEDLINE]
Free PMC Article
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