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Determinants that enable disordered protein assembly into discrete condensed phases
Cells spatially organize biochemical reactions within membrane-bound and membraneless compartments. The extent to which intrinsically disordered proteins themselves can form discrete compartments or condensed phases is poorly understood. Now a pair of model IDRs that display orthogonality in condensation and the chain features governing selective assembly have been identified.
- Rachel M. Welles
- , Kandarp A. Sojitra
- & Matthew C. Good
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Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains
The complex link between protein sequence and phase behaviour for a family of prion-like low-complexity domains (PLCDs) has now been revealed. The results have uncovered a set of rules—which are interpreted using a stickers-and-spacers model—that govern the sequence-encoded phase behaviour of such PLCDs and enable physicochemical rationalizations that are connected to the underlying sequence composition.
- Anne Bremer
- , Mina Farag
- & Tanja Mittag