The use of Boresch restraints, instead of the Euler and polar angles employed in the original geometrical route framework, 67 makes the implementation of our approach straightforward in most MD packages. The use of helical and RMSD restraints significantly accelerates the convergence of the free energy calculations and avoids artefacts commonly observed in implicit solvent modelling of interactions between charged side chains, which are frequently found in coiled coils. The viability of our protocol with implicit solvent force fields is of particular importance for its applicability to protein design pipelines, which require computationally efficient protocols to screen large numbers of designs. We have shown that our approach can successfully recover the preferred topological arrangement of different coiled coils in a given oligomerisation state, the preferred oligomerisation state of different coiled coils, and pH-dependent conformational effects. Our approach could be used to assess the viability of designs produced by faster, but less accurate, parametric design pipelines, thereby increasing the likelihood of success in multi-state protein design efforts.