In the following, it is shown that the OLIVES Gō-like model excellently reproduces in-tramolecular native contacts in line with the established structure-biased method of the GoMARTINI Gō-like model, even in proteins with a large fraction of hydrophobic contacts not explicitly treated by OLIVES. Furthermore, we find that OLIVES can stabilize the Martini 3 protein model without using DSSP secondary structure restraints. We demonstrate that OLIVES reduces the number of bias potentials, which speeds up simulations by up to ≈ 30 % on GPU hardware compared to the GoMARTINI Gō-like model. We also show that the stability of solution protein complexes cannot be reproduced without using a quaternary bias network, while transmembrane protein complexes are stable in line with previous work. We conclude the paper with a discussion of the underlying reasons why the stability of Martini 3 solution complexes is underestimated and discuss future directions for the improvement of the Martini 3 protein model.