Fig. 3

CSB directly binds N-terminal and NAC regions of α-synuclein. a Superposition of ¹H-¹⁵N HSQC spectra of α-synuclein (80 μM) alone (blue) and in the presence of a fivefold molar excess of CSB (red). Strong signal attenuation together with chemical shift changes were observed for select residues. b Residue-specific changes in the intensities of ¹H-¹⁵N HSQC cross-peaks of α-synuclein induced at increasing concentrations of CSB. I₀ and I are the intensities of ¹H-¹⁵N HSQC cross-peaks in the absence and presence of CSB, respectively. c Intensity changes (I–I₀) of non-overlapping residues at the N-terminus of α-synuclein reflecting exchange behavior show prominent slowing on the NMR chemical shift scale in the presence of increasing concentrations of CSB. Lines represent global fits to the experimental data for all selected residues based on a reversible 1-to-1 binding model