The interface between biomolecular condensates and their surrounding (aqueous) phase plays an important role for, e.g., stabilizing the condensates1 and for regulating the interactions with other cellular components2. These functions likely depend on the specific composition and conformations of proteins on the surface, which are difficult to probe through in vitro experiments. To shed light on this challenging question, Farag et al. employed lattice-based Monte Carlo (MC) simulations of various prion-like low-complexity domains (LCDs)3, focusing on the wild-type sequence of A1-LCD. One of their key findings was that this class of proteins formed expanded conformations at the droplet-water interface, which stretch out into the surrounding aqueous phase. Interestingly, Farag et al. found similar results even for hydrophobic homopolymers (see Fig. S15f in Ref. 3). These results are quite surprising, since we expected a gradual collapse of the chains moving from the bulk-like droplet interior to the surrounding poor solvent4,5,6, because the effective solvent quality should decrease monotonically with decreasing local polymer concentration7.