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. Author manuscript; available in PMC: 2020 Sep 9.
Published in final edited form as: Nat Chem Biol. 2020 Mar 9;16(6):653–659. doi: 10.1038/s41589-020-0480-6

Fig. 5 |. Topology of α-synuclein–membrane interactions.

Fig. 5 |

a, α-Synuclein’s hydrophobic residues (repeat position 2 shown as spheres) wind around an idealized α-helix ([φ, ψ] = [–57°, −47°], 3.60 residues/turn). b, Hypothetical model of α-synuclein interacting with membranes of negative Gaussian curvature, which is consistent with both NMR spectroscopy in the presence of anionic membranes of native-like composition16,39, as well as functional data in neurons45. Membrane-contacting residues (repeat positions 2, 6, 9, 10) shown as blue spheres.