Resonance assignments of an α-synuclein fibril prepared in Tris buffer at moderate ionic strength.

ABSTRACT: Fibrils of the protein α-synuclein (α-syn) are implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders. We have reported a high-resolution structure (PDB 2N0A) of an α-syn fibril form prepared by in vitro incubation of monomeric protein in 50 mM sodium phosphate buffer pH 7.4 with 0.1 mM EDTA and 0.01% sodium azide. In parallel with this structure determination, ongoing studies of small molecule ligands binding to α-syn fibrils, prepared in 2-amino-2-(hydroxymethyl)-1,3-propanediol (Tris) buffer, have been in progress, and it is therefore of interest to determine the structural similarity of these forms. Here we report the ¹³C and ¹⁵N resonance assignments for α-syn fibrils prepared with Tris-HCl buffer (pH 7.7 at 37 °C) and 100 m

SUBMITTER: Barclay AM 

PROVIDER: S-EPMC5877819 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature