Interestingly, there have been recent studies of Martini 3 applied to intrinsically disordered proteins (IDPs), suggesting that either protein-protein interactions are too strong or, alternatively, that protein-water interactions are too weak. It has been clearly shown that either downscaling protein-protein interactions or upscaling protein-water interactions can reconcile simulation results with experimental results of IDPs and proteins with disordered regions. Perplexingly, both of these approaches would further destabilize solution protein complexes, which strongly suggests that a flat scaling of either protein-protein or protein-water interactions cannot be a general solution, even though it is useful to the spe-cific application of simulating IDPs. Further complicating matters, there have also been conflicting reports that protein-water interactions need to be downscaled by 10 % for proper insertion of transmembrane helices into self-assembled phospholipid bilayers and micelles. The conflicting studies of flat scaling of protein-water interactions hint that the Martini 3 protein model still has room for improvement, and in the following, we want to direct attention to some areas where the current description of proteins in Martini 3 could be enhanced, with a particular focus on soluble protein-protein complexes.