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Phase separation of intrinsically disordered proteins is important for theformation of membraneless organelles, or biomolecular condensates, which playkey roles in the regulation of biochemical processes within cells. In thiswork, we investigated the phase separation of different sequences of acoarse-grained model for intrinsically disordered proteins and discovered asurprisingly rich phase behavior. We studied both the fraction of totalhydrophobic parts and the distribution of hydrophobic parts. Not surprisingly,sequences with larger hydrophobic fractions showed conventional liquid-liquidphase separation. The location of the critical point was systematicallyinfluenced by the terminal beads of the sequence, due to changes in interfacialcomposition and tension. For sequences with lower hydrophobicity, we observednot only conventional liquid-liquid phase separation, but also reentrant phasebehavior, in which the liquid phase density decreases at lower temperatures.For some sequences, we observed formation of open phases consisting ofaggregates, rather than a normal liquid. These aggregates had overall lowerdensities than the conventional liquid phases, and exhibited complex geometrieswith large interconnected string-like or membrane-like clusters. Our findingssuggest that minor alterations in the ordering of residues may lead to largechanges in the phase behavior of the protein, a fact of significant potentialrelevance for biology.

Model for disordered proteins with strongly sequence-dependent liquid phase behavior