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Biomolecular condensates undergirded by phase separations of proteins andnucleic acids serve crucial biological functions. To gain physical insightsinto their genetic basis, we study how liquid-liquid phase separation (LLPS) ofintrinsically disordered proteins (IDPs) depends on their sequence chargepatterns using a continuum Langevin chain model wherein each amino acid residueis represented by a single bead. Charge patterns are characterized by the`blockiness' measure $\kappa$ and the `sequence charge decoration' (SCD)parameter. Consistent with random phase approximation (RPA) theory and latticesimulations, LLPS propensity as characterized by critical temperature $T^*_{\rmcr}$ increases with increasingly negative SCD for a set of sequences showing apositive correlation between $\kappa$ and $-$SCD. Relative to RPA, thesimulated sequence-dependent variation in $T^*_{\rm cr}$ is often---though notalways---smaller, whereas the simulated critical volume fractions are higher.However, for a set of sequences exhibiting an anti-correlation between $\kappa$and $-$SCD, the simulated $T^*_{\rm cr}$'s are quite insensitive to eitherparameters. Additionally, we find that blocky sequences that allow for strongelectrostatic repulsion can lead to coexistence curves with upward concavity asstipulated by RPA, but the LLPS propensity of a strictly alternating chargesequence was likely overestimated by RPA and lattice models because interchainstabilization of this sequence requires spatial alignments that are difficultto achieve in real space. These results help delineate the utility andlimitations of the charge pattern parameters and of RPA, pointing to furtherefforts necessary for rationalizing the newly observed subtleties.

Coarse-Grained Residue-Based Models of Disordered Protein Condensates: Utility and Limitations of Simple Charge Pattern Parameters