On the transient interactions of α-synuclein in different dimensions
α-Synuclein (αSyn) is a neuronal protein predominantly found in the brain, whose native function seems to be associated with vesicle trafficking. While intrinsically disordered in solution, the first ca. 100 residues adopt an amphipathic α-helical structure when the protein adsorbs onto membranes. Additionally, the aggregation of αSyn into highly ordered β-sheet rich amyloid fibrils is associated
