Abstract
Intrinsically disordered proteins (IDPs) are nowadays recognized as ubiquitous components of the cell, extending the structure-function relationship towards multiple structure-function relationships. One such famous IDP is α-synuclein (α-syn) that can fold in helical structures when interacting with membranes to support dopamine-containing vesicles but can change conformation towards beta strand-based structures that promote its self-association towards forming oligomers and amyloid fibrils somehow associated with the intracellular pathophysiology of Parkinson's disease (PD).
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