Before revision:  Three different residue-residue interaction schemes sharing the same electrostatic potentialwere evaluated. We found that neither a common scheme based on amino acid hydrophobicity nor one augmented with arginine/lysine-aromatic cation-\pi interactions can consistently account for the available experimental LLPS data on the wildtype, a charge-scrambled mutant, a phenylalanine-to-alanine (FtoA) mutant and an arginine-to-lysine (RtoK ) mutant of the Ddx4 IDR.
After revision:  Three different residue-residue interaction schemes with a shared electrostatic potential. Neither a common hydrophobicity scheme nor one augmented with arginine/lysine-aromatic cation-\pi interactions can consistently account for the available experimental LLPS data on the wildtype, a charge-scrambled mutant, a phenylalanine-to-alanine (FtoA) mutant and an arginine-to-lysine (RtoK ) mutant of the Ddx4 IDR.