Before revision:  Endeavoring toward a transferable, predictive coarse-grained explicit-chain model for biomolecular LLPS, we used the N-terminal intrinsically disordered region (IDR) of the DEAD-box helicase Ddx4  as a test case to conduct extensive multiple-chain simulations to assess the roles of electrostatic, hydrophobic, cation-\pi, and aromatic interactions in sequence-specific phase behaviors. Three different residue-residue interaction schemes sharing the same electrostatic potentialwere evaluated.
After revision:  Endeavoring toward a transferable, predictive coarse-grained explicit-chain model for biomolecular LLPS, we used the N-terminal intrinsically disordered region (IDR) of the DEAD-box helicase Ddx4 as a test case to conduct extensive multiple-chain simulations to assess the roles of electrostatic, hydrophobic, cation-\pi, and aromatic interactions in amino acid sequence-dependent LLPS. We evaluated 3 residue-residue interaction schemes sharing the same electrostatic potentialwere evaluated.