We validate the ability of OLIVES to stabilize known protein complexes situated both in solution and in phospholipid bilayers. By comparing to atomistic simulations of the same complexes, we address the open question of whether there is a need for protein quaternary structure bias in Martini 3 simulations. Oligomerization studies are commonly performed using Martini; however, these are often between transmembrane proteins, perhaps because Martini started as a phospholipid force field. However, oligomerization between soluble proteins has been less studied using Martini 3, and an assessment of the ability of Martini 3 to stabilize known protein partners in both the solution phase and in bilayers is therefore needed. Specifically, because the tertiary structure in Martini is unstable, it is likely that quaternary structure stability is also underestimated since the underlying physical interaction principles are the same.