Liquid–Liquid Phase Separation As the Second Step of Complex Coacervation

Liquid-liquid phase separation (LLPS) between tyrosine- and arginine-rich peptides are of biological importance. To understand the interactions proteins in condensed close analogy to complex coacervation, we run multiple umbrella calculations oligomers containing tyrosine (pY) arginine (pR). We find pR-pY complexation be energetically driven. Metadynamics simulations on monomers suggest that this energy is correlated with number ?-cation bonds. Free for binding pairs poly glutamate-pR dimers show striking similarities process LLPS. These residues do not undergo followed by coacervation. The mechanism, rather, akin neutral polyion pairs.