The notion that many dynamic and transient interactions between different amino acid residues work in tandem to drive biomolecular condensate formation is also supported by a recent combined experimental and all-atom MD simulation study of Rekhi et al., who investigated the (GRGDSPYS) 25 repeat polypeptide and different variants of it . Simulations of 30 polypeptide chains in a slab geometry showed that contacts involving the traditional spacer amino acids Ser and Gly were very frequent, in addition to contacts between canonical stickers such as Tyr and Arg, Tyr with itself, and electrostatic interactions of Arg and Asp. These results thus extend the canonical stickers-and-spacers picture and underline the relevance also of interactions mediated by uncharged, nonaromatic residues in driving LLPS . Rekhi et al. also investigated whether the molecular interactions that drive condensate formation are different from the ones that stabilize the condensate once it has formed. The authors showed that the residue-residue contacts formed in single-chain simulations are strongly correlated with the contacts found in the condensate, underlining the similarity of the molecular interactions at play . These results are in line with previous studies showing that chain dimensions or solvent quality can provide knowledge on LLPS -collapsed polypeptide chains are more prone to phase separation. Therefore, trends on the PS tendency can be deduced from simulations of single chains in solution .