Extended Data Fig. 9: Sequence-specific NMR-resonance assignments of methionine-oxidized and tyrosine-phosphorylated α-synuclein variants.
From: Regulation of α-synuclein by chaperones in mammalian cells
a–c, Two-dimensional [15N, 1H]-NMR spectra of 100 µM oxidized [U-15N]-α-synuclein (light grey), 100 µM oxidized [U-15N]-acetyl-α-synuclein (violet) and 100 µM oxidized [U-15N]-ΔN-α-synuclein (blue). The sequence-specific resonance assignments from chemical-shift mapping and published assignments of the oxidized state23 are indicated. Oxidized methionines are highlighted in red. d, Residue-resolved combined chemical-shift differences of the amide moieties for oxidized α-synuclein (light grey), oxidized acetyl-α-synuclein (violet) and oxidized-ΔN-α-synuclein (blue) relative to their respective reduced states. Colours as in a–c. Arrows indicate the positions of the oxidized methionines. e–g, Two-dimensional [15N, 1H]-NMR spectra of 50 µM [U-15N]-mono-phospho-α-synuclein (red-brown), 50 µM [U-15N]-tri-phospho-α-synuclein (brown) and 50 µM [U-15N]-tetra-phospho-α-synuclein (dark brown). The sequence-specific resonance assignments based on published assignments for phosphorylated α-synuclein are indicated24. Phosphorylated residues are highlighted in cyan. h, Residue-resolved combined chemical-shift differences of the amide moieties for the phosphorylated α-synuclein variants relative to wild-type α-synuclein. Colours as in e–g. Arrows indicate the positions of the phosphorylated tyrosines. [15N, 1H]-NMR spectra of the different modified α-synuclein variants were measured several times (n = 4) yielding similar results.
