to have played roles in primitive RNA metabolism and folding. Specific AA sequences are also required for proper folding and structure in structured proteins. Abiotic, potentially error-prone synthesis of peptides during the OOL could have led to the random, non-specific addition of AAs in primitive peptides, potentially lead to the formation of unfolded disordered peptides on early Earth containing domains like RGG. As RGG domains themselves can potentially phase separate in vitro, the formation of primitive coacervates composed of primordial short-disordered RGG and/or RGG-containing peptides bound to other biomolecules (like primitive nucleic acids) is certainly plausible.