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An ensemble-based model in which pre-existing conformational organization shapes how the protein responds to the matched mutations is supported and stability-engineering mutations should be evaluated in the context of the parent ensemble is argued.
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...
A two-layer regulatory mechanism in which phosphorylation rewires IDR electrostatics while pocket-binding ligands redirect folded-domain interactions is revealed, suggesting a strategy for modulating multidomain condensates through ligand-induced contact-network remodeling.
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