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Liquid-liquid phase separation of intrinsically disordered proteins (IDPs) isa major undergirding factor in the regulated formation of membranelessorganelles in the cell. The phase behavior of an IDP is sensitive to its aminoacid sequence. Here we apply a recent random-phase-approximation polymer theoryto investigate how the tendency for multiple chains of a protein to phaseseparate, as characterized by the critical temperature $T^*_{\rm cr}$, isrelated to the protein's single-chain average radius of gyration $\langleR_{\rm g} \rangle$. For a set of sequences containing different permutations ofan equal number of positively and negatively charged residues, we found astriking correlation $T^*_{\rm cr}\sim \langle R_{\rm g} \rangle^{-\gamma}$with $\gamma$ as large as $\sim 6.0$, indicating that electrostatic effectshave similarly significant impact on promoting single-chain conformationalcompactness and phase separation. Moreover, $T^*_{\rm cr}\propto -{\rm SCD}$,where SCD is a recently proposed "sequence charge decoration" parameterdetermined solely by sequence information. Ramifications of our findings fordeciphering the sequence dependence of IDP phase separation are discussed.

Phase separation and single-chain compactness of charged disordered proteins are strongly correlated