Abstract
Large aggregates of the intrinsically disordered protein α-synuclein, known as Lewy bodies, are one of the key indicators of Parkinson’s disease (PD). They can occur in both solution and in the membrane, and form by the oligomerization and fibrilization of misfolded α-synuclein proteins. The α-synuclein protein consists of three distinct protein domains: an amphipathic N-terminal region, the hydrophobic core NAC region, and the proline rich C-terminal region. Within Lewy bodies, most α-synuclein proteins show a truncated C-terminal domain, and removal of the domain has been shown to increase the propensity for aggregation.
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