RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins
Fig 5
(a) Phase diagram in the temperature–density plane for a scaffold protein that, like FUS, can phase separate via homotypic protein interactions (black curve), and for mixtures of a fixed RNA/protein concentration using different RNA strand lengths as indicated in the legend. (b) Phase diagram in the temperature-density plane for a cognate protein that, like PR25, does not exhibit LLPS on its own, and that only undergoes LLPS upon addition of RNA. The RNA concentration in both panels was kept constant in all simulations at a 0.25 nucleotide/protein ratio. Filled circles represent the coexisting densities evaluated from DC simulations, while empty circles depict the critical temperatures estimated from the law of rectilinear diameters and critical exponents near the critical temperature [119]. The error bars in the coexistence densities represent the standard deviation, while those of the critical points represent the extrapolated uncertainty when applying the law of rectilinear diameters and critical exponents. Temperature in both panels has been normalized by the critical temperature of the pure scaffold system, in reduced units (empty black circle in (a)).