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Yet another polymorph of ?-synuclein: solid-state sequential assignments.
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Biomol NMR Assign 2013 Oct;
Authors: Julia Gath, Luc Bousset, Birgit Habenstein, Ronald Melki, Beat H Meier, Anja BŲckmann
Physical Chemistry, ETH ZŁrich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
Parkinson's disease is a neurological human proteinopathy, which is caused by the accumulation of protein aggregates of high molecular mass. ?-Synuclein is a major component of these fibrillar, ?-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. ?-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 ?-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 ?-sheet. The chemical shifts differ substantially from the polymorph we previously assigned.
PMID: 24114178 [PubMed - as supplied by publisher]