Resonance assignments of an α-synuclein fibril prepared in Tris buffer at moderate ionic strength
| Autor: | Chad M. Rienstra, Joseph M. Courtney, Dhruva Dhavale, Paul T. Kotzbauer, Alexander M. Barclay |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Tris Protein Data Bank (RCSB PDB) macromolecular substances 010402 general chemistry Fibril 01 natural sciences Biochemistry Protein Structure Secondary Article 03 medical and health sciences chemistry.chemical_compound Structural Biology Hydroxymethyl Nuclear Magnetic Resonance Biomolecular Osmolar Concentration Phosphate 0104 chemical sciences Crystallography 030104 developmental biology Monomer chemistry Ionic strength alpha-Synuclein Sodium azide Protein Multimerization |
| Zdroj: | Biomolecular NMR Assignments. 12:195-199 |
| ISSN: | 1874-270X 1874-2718 |
| Popis: | Fibrils of the protein α-synuclein 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-synuclein 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-synuclein 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 (13)C and (15)N resonance assignments for α-synuclein fibrils prepared with Tris-HCl buffer (pH 7.7 at 37°C) and 100 mM NaCl. These fibrillization conditions yield a form with fibril core chemical shifts highly similar to those we reported (BMRB 16939) in the course of determining the high-resolution 2N0A structure, with the exception of some small perturbations from T44 to V55, including two sets of peaks observed for residues T44 to V48. Additional differences occur in the patterns of observed residues in the primarily unstructured N-terminus. These results demonstrate a common fold of the fibril core for α-synuclein fibrils prepared in phosphate or Tris-HCl buffer at moderate ionic strength. |
| Databáze: | OpenAIRE |
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