Extended Data Fig. 6 | LUVs and the chaperone SecB compete for α-synuclein
binding. a, Residue-resolved backbone amide NMR signal attenuation
(Irel = I/I 0 ) of α-synuclein caused by the addition of 5 mg ml−1 LUVs (125:1 molar
ratio of lipid:protein; dark yellow) and after further addition of 2 equivalents of
SecB (yellow). b, Residue-resolved backbone amide NMR signal attenuation
(Irel = I/I 0 ) of α-synuclein caused by the addition of 15 mg ml−1 LUVs (375:1 molar
ratio lipid:protein; dark yellow) and after further addition of 2 and 6 equivalents
of SecB, respectively (yellow), measured at 298 K. c, Residue-resolved
backbone amide NMR signal attenuation (Irel = I/I 0 ) of α-synuclein caused by the
addition of 2 equivalents of SecB (yellow) and increasing amounts of LUVs with
the following ratios: 2.5 mg ml−1, 62.5:1; 4.0 mg ml−1, 100:1; 6.25 mg ml−1, 156:1;- 5 mg ml−1, 212.5:1. d, Schematic showing the conformational equilibrium of
free α-synuclein, its chaperone-bound state and one possible conformation of
its LUV-bound state (PDB 1XQ8)^19. Notably, these observations are also in full
agreement with related studies for HSP90^12 and HSP27^37. e, Dynamic light
scattering (DLS) measurements of LUVs prepared from pig brain polar lipids.
Two independent preparations are shown in blue and orange, respectively, with
an average diameter of 110 nm.