PARCL is an RNA-binding protein (RBP) that exhibits chaperone activity, is abundant in the phloem, intrinsically disordered, and contains a prion-like domain (PLD). PARCL proteins have been observed to form large biomolecular condensates in vivoand in vitro. Biomolecular condensates are membraneless compartments, wherein biomolecules become partitioned from their surrounding liquid environment into liquid droplets with their own composition, dynamics, and function. We present recent results derived from simulation of PARCL using course-grained molecular dynamics with the HPS-Urry model. Phase separation simulations have not previously included fluorescent tags which are often used in phase separation experiments for visualising droplets. We adjust the parameters of the simulations to allow the inclusion of folded eYFP tags and while still simulating phase separation, these trajectories suggest changes to droplet and network structure when proteins contain eYFP. By analysing the residues of the PARCL molecules that make contact in the simulations, we identify which individual residues drive the phase separation. We experimentally validate these findings by mutation of the most contacted residues, which prevents the formation of condensate droplets. To investigate the RNA-binding of PARCL we add microRNA to the simulation and find a short region of PARCL consistently making contact with the miRNA. We discuss the implications of our findings in terms of model-guided engineering of biomolecular condensates.