Extended Data Fig. 8: Sequence-specific NMR-resonance assignments of α-synuclein variants.
From: Regulation of α-synuclein by chaperones in mammalian cells
a–c, Two-dimensional [15N, 1H]-NMR spectra of 500 µM [U-13C, 15N]-α-synuclein (grey), 450 µM [U-13C, 15N]-acetyl-α-synuclein (dark violet) and 100 µM [U-15N]-∆N-α-synuclein (dark blue). The sequence-specific resonance assignments for wild-type as well as acetylated α-synuclein obtained from three-dimensional triple resonance experiments and from chemical-shift mapping of ΔN-α-synuclein are indicated. d, e, Two-dimensional [13C, 15N]-NMR spectra of 500 µM [U-13C, 15N]-α-synuclein (grey) and 450 µM [U-13C, 15N]-acetyl-α-synuclein (dark violet). The sequence-specific resonance assignments for wild-type and acetylated α-synuclein obtained from three-dimensional triple resonance experiments are indicated. f, Residue-resolved combined chemical-shift perturbations of the amide moieties for acetyl-α-synuclein (dark violet) and ΔN-α-synuclein (dark blue) versus wild-type α-synuclein. g, Residue-resolved combined chemical-shift difference of the carbonyl-amide moieties for acetyl-α-synuclein (dark violet) versus wild-type α-synuclein. [15N, 1H]-NMR spectra in a–c were measured five times and [13C, 15N]-NMR spectra (d, e) were measured in duplicates, all yielding similar results.
