The studies discussed above focused on protein-only systems. But many biomolecular condensates are multicomponent coacervates involving proteins and nucleic acids, among other molecules. To investigate the intricate interplay of homotypic and heterotypic interactions in such systems, Unarta et al. performed thousands of short all-atom MD simulations (accumulated simulation time of more than a ms) of model condensates formed by a scaffold RNA oligomer and an arginine-rich peptide . The studied model condensates contained one of three possible peptides, the scaffold peptide itself or variants in which six arginines were either replaced by lysine or by asymmetric dimethyl arginine (ADMA). The Arg-rich peptide can form the largest number of hydrogen bonds and bind the strongest to the scaffold RNA. There was no significant difference in the number of cation-π interactions between the Arg-rich peptide and the scaffold RNA compared to the Lys-rich and ADMA-rich peptides, indicating that hydrogen bonds between the peptides and the RNA backbone rather than cation-π interactions play a major role in the condensate .