- Journal Article
Rights / licenseIn Copyright - Non-Commercial Use Permitted
Parkinson’s disease is a neurological human proteinopathy, which is caused by the accumulation of protein aggregates of high molecular mass. α-Synuclein is a major component of these fibrillar, β-sheet rich, insoluble assemblies and is deposited in the form of amyloids. Structural characterization of amyloids is possible by solid-state NMR, although no atomic-resolution structure is available as of today. α-Synuclein, as many other pathology-related fibril-forming proteins, can form a number of different polymorphs that are sometimes tricky to obtain in pure form. Here, we describe the chemical shifts and secondary structure analysis of a polymorph that also adopts mainly β-sheet conformation, with a fibrillar core ranging from residues 38 to 94. In addition, residues 15–20 from the N-terminus found to be part of a rigid ordered β-sheet. The chemical shifts differ substantially from the polymorph we previously assigned. Show more
Journal / seriesBiomolecular NMR Assignments
Pages / Article No.
Subjectα-Synuclein; Fibrils; Solid-state NMR; Assignments; Secondary structure
Organisational unit03496 - Meier, Beat H. / Meier, Beat H.
NotesIt was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
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