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Default Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.

Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.

Related Articles Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.

Biomol NMR Assign. 2016 May 10;

Authors: Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH

Abstract
The formation of fibrils of the amyloid-? (A?) 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?(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.


PMID: 27165577 [PubMed - as supplied by publisher]



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