The computational efficiency of coarse-grained methods allows one to tackle large-scale simulation systems on extended timescales, and thus to minimize finite box-size effects and to obtain statistically precise results. However, by construction, such CG models cannot inform us about the atomic-level details of the molecular interactions and structural dynamics at play. This limitation does not only concern the biomolecules themselves, but in particular also the solvent, which in CG models is either implicitly included or, if explicitly represented as particles, it is described as a simple Lennard-Jones fluid. Therefore, to obtain detailed and accurate insights into solvation effects atomistic water models have to be employed, as is done in all-atom simulations with explicit solvent. However, due to the strongly increased computational demands, the timescales needed to describe the process of condensate formation are out of reach for all-atom simulations, and preformed condensates are investigated instead. Pioneering all-atom MD simulation studies of such preformed biocondensates were carried out by Rauscher and Pomès for elastin-like peptides and by Zheng et al. for the disordered domain of LAF-1 and the low complexity domain (LCD) of the human fused in sarcoma (FUS) protein .