Membrane association places α-synuclein (αSyn) at the boundary between physiological surface organization and pathological amyloid assembly, supporting vesicle clustering, surface condensation, and amyloid nucleation. How interfacial recruitment, condensate cohesion, and persistent amyloid-like organization are coupl...
Intrinsically disordered proteins (IDPs) form biomolecular condensates through weak multivalent interactions, but the ensemble variables that control condensate stability and material properties remain incompletely defined. Most current descriptions emphasize sequence features or mean single-chain descriptors, such a...
Ci-Bo Feng, Shiqinrui Xu, Hai-Bin Su et al.· JACS Au· 0 citations
Biomolecular condensates formed by multidomain proteins are increasingly linked to disease and are emerging targets for chemical modulation. Yet most molecular models emphasize intrinsically disordered regions (IDRs), whereas many available ligands bind folded-domain pockets. How IDR modifications and folded-domain lig...