The N-Terminal Residues 43 to 60 Form the Interface for Dopamine Mediated α-Synuclein Dimerisation
Fig 7
Chemical shift deviations between DA:α-syn 43–140 monomer and DA:α-syn 43–140 dimer.
The Cα resonances (Panels A and B) of the DA:α-syn 43–140 dimer do not differ significantly from those of the DA:α-syn 43–140 monomer. A. Cα chemical shift deviations from random coil values predict that the DA:α-syn 43–140 monomer is largely unstructured. B. Plot of chemical shift difference for Cα chemical shifts between DA:α-syn 43–140 monomer and DA:α-syn 43–140 dimer. The chemical shift deviation is plotted in ppm as a function of residue position in DA:α-syn 43–140 monomer. C. Plot of difference in Cα resonance position (ΔδCα (ppm)) from random coil values [60] for DA:α-syn 43–140 monomer. The largest differences arise from residues preceding a proline (A107, M116, D119, M127, E138). D. Plot of difference in Cα resonance positions between DA:α-syn 43–140 monomer and DA:α-syn 43–140 dimer (δdimer—δmonomer). The absence of significant chemical shift differences between the DA:α-syn 43–140 dimer and DA:α-syn 43–140 monomer indicates their structural similarity. The largest differences are localised to residues near the methionine residues (M116, M127) that are likely to be oxidised under the conditions of DA-mediated α-syn 43–140 dimer formation.