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. 2016 Jan 25;7:10251. doi: 10.1038/ncomms10251

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(a) The amino-acid sequence of α-Syn residues flanking Met127. Ser129 and Tyr125 phosphorylation sites are highlighted. (b) Real-time NMR profiles of Tyr125 phosphorylation kinetics of reduced and methionine-oxidized, N-terminally acetylated α-Syn in reconstituted kinase reactions with recombinant Fyn. (c) Real-time NMR profiles of Ser129 phosphorylation kinetics of reduced and methionine-oxidized, N-terminally acetylated α-Syn in reconstituted kinase reactions with recombinant Plk3. Error bars represent the average experimental noise of the respective 2D NMR spectra. Phosphorylation behaviours were confirmed on two independent samples for each kinase.