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The recently proposed Hamiltonian Adaptive Resolution Scheme (H-AdResS)allows to perform molecular simulations in an open boundary framework. Itallows to change on the fly the resolution of specific subset of molecules(usually the solvent), which are free to diffuse between the atomistic regionand the coarse-grained reservoir. So far, the method has been successfullyapplied to pure liquids. Coupling the H-AdResS methodology to hybrid models ofproteins, such as the Molecular Mechanics/Coarse-Grained (MM/CG) scheme, is apromising approach for rigorous calculations of ligand binding free energies inlow-resolution protein models. Towards this goal, here we apply for the firsttime H-AdResS to two atomistic proteins in dual-resolution solvent, proving itsability to reproduce structural and dynamic properties of both the proteins andthe solvent, as obtained from atomistic simulations.

Open Boundary Simulations of Proteins and Their Hydration Shells by Hamiltonian Adaptive Resolution Scheme