Abstract
Liquid-liquid phase separation (LLPS) of intrinsically disordered proteins/regions (IDPs/IDRs) into intracellular biomolecular condensates is involved in critical cellular functions. However, aberrant phase transitions are associated with debilitating neurodegenerative diseases. We show that the prion protein (PrP) can undergo LLPS via weak, multivalent, transient intermolecular interactions between the N-terminal IDR that resembles a yeast prion-like domain comprising five glycine-rich octapeptide repeats and a hydrophobic segment.
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