['Empirical binding models have previously been investigated for the energetics of protein complexation (DeltaG models) and for the influence of mutations on complexation (i.e. differences between wild-type and mutant complexes, DeltaDeltaG models). We construct binding models to directly compare these processes, which have generally been studied separately.', 'Although reasonable fit models were found for both DeltaG and DeltaDeltaG cases, they differ substantially. In a dataset curated for the absence of mainchain rearrangement upon binding, non-polar area burial is a major determinant of DeltaG models. However this DeltaG model does not fit well to the data for binding differences upon mutation. Burial of non-polar area is weighted down in fitting of DeltaDeltaG models. These calculations were made with no repacking of sidechains upon complexation, and only minimal packing upon mutation. We investigated the consequences of more extensive packing changes with a modified mean-field packing scheme. Rather than emphasising solvent exposure with relatively extended sidechains, rotamers are selected that exhibit maximal packing with protein. This provides solvent accessible areas for proteins that are much closer to those of experimental structures than the more extended sidechain regime. The new packing scheme increases changes in non-polar burial for mutants compared to wild-type proteins, but does not substantially improve agreement between DeltaG and DeltaDeltaG binding models.'] Do volume-based solvation models out-perform area-based models in combined studies of wild-type and mutated protein-protein interfaces?