Revealing condensation affinities of multivalent protein residues through atomistic simulation of model peptide mixtures.

Bio-molecular condensation of proteins has emerged as a key mechanism underlying the formation of membraneless cellular bodies. The thermodynamic driving force of condensation is often rationalized from the perspective of polymeric liquid-liquid phase separation and classical mean-field theories. However, the environment of biomolecular condensates often deviates from the mean-field picture and requires a more detailed microscopic model of intra and inter-residue interactions within condensates. In this work, we set up model peptide mixtures, which allows one to quantify the affinity of different residue-base pairs under various external and internal conditions, including salt, stoichiometry, density, and temperature.