Currently, the computational cost of explicit solvent simulations prevents their routine use in protein design pipelines. The use of implicit solvent models is therefore highly desirable for protein design purposes, due to its high computational efficiency and faster conformational sampling compared to explicit solvent. However, implicit solvent models have been deemed insufficient for accurately reproducing the secondary structure preferences of peptides, 101-103 particularly peptides with a high content of charged residues, due to their tendency to produce salt-bridge-trap conformations. 101-108 Nevertheless, while coiled coils have a considerable number of native salt bridges, which may be mistreated with an implicit solvent model, the main driving force for coiled coil assembly is the hydrophobic effect, which can be adequately modelled with implicit solvent. Additionally, the use of conformational, orientational and positional restraints during the binding free energy calculations precludes the formation of non-native salt bridges.