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A fully atomistic modelling of biological macromolecules at relevant length-and time-scales is often cumbersome or not even desirable, both in terms ofcomputational effort required and it a posteriori analysis. This difficulty canbe overcome with the use of multi-resolution models, in which different regionsof the same system are concurrently described at different levels of detail. Inenzymes, computationally expensive atomistic detail is crucial in the modellingof the active site in order to capture e.g. the chemically subtle process ofligand binding. In contrast, important yet more collective properties of theremainder of the protein can be reproduced with a coarser description. In thepresent work, we demonstrate the effectiveness of this approach through thecalculation of the binding free energy of hen egg white lysozyme (HEWL) withthe inhibitor di-N-acetylchitotriose. Particular attention is posed to theimpact of the mapping, i.e. the selection of atomistic and coarse-grainedresidues, on the binding free energy. It is shown that, in spite of smallvariations of the binding free energy with respect to the active siteresolution, the separate contributions coming from different energetic terms(such as electrostatic and van der Waals interactions) manifest a strongerdependence on the mapping, thus pointing to the existence of an optimal levelof intermediate resolution.

Ligand-protein interactions in lysozyme investigated through a dual-resolution model