Having simulated both soluble and transmembrane protein complexes, we observe an apparent trend that solution complexes are not stable and transmembrane complexes are. We have simulated 4 additional solution complexes, including the human leukemia inhibitory factor in complex with the gp130 domain (PDB: 1PVH), human cyclophilin A bound to the HIV-1 capsid (PDB: 1AK4), the E. coli methionine apo-repressor homodimer (PDB: 1MJM), and mouse nerve growth factor homodimer (PDB: 5LSD), which all follow the same trend of being stable in atomistic simulations but quickly dissociate in Martini 3 simulations without a quaternary bias network, irrespective of the intrachain Gō-like model used. Taken together, this is evidence that protein intermolecular interactions for solution complexes are not stable in the current implementation of Martini 3 proteins. This would be expected from the observation that tertiary structures are not stable. However, as we observe transmembrane dimers to be stable, we speculate that protein-protein interactions are somewhat balanced (with respect to the lipids). Instead, imbalances in protein-water interactions could lead to an underestimation of the hydrophobic effect, destabilizing solution complexes like the Ubiquitin/UBA domain system.