% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Tarenzi:838466,
      author       = {Tarenzi, Thomas and Calandrini, Vania and Potestio,
                      Raffaello and Giorgetti, Alejandro and Carloni, Paolo},
      title        = {{O}pen {B}oundary {S}imulations of {P}roteins and {T}heir
                      {H}ydration {S}hells by {H}amiltonian {A}daptive
                      {R}esolution {S}cheme},
      journal      = {Journal of chemical theory and computation},
      volume       = {13},
      number       = {11},
      issn         = {1549-9626},
      address      = {Washington, DC},
      reportid     = {FZJ-2017-07069},
      pages        = {5647–5657},
      year         = {2017},
      abstract     = {The recently proposed Hamiltonian Adaptive Resolution
                      Scheme (H-AdResS) allows to perform molecular simulations in
                      an open boundary framework. It allows to change on the fly
                      the resolution of specific subset of molecules (usually the
                      solvent), which are free to diffuse between the atomistic
                      region and the coarse-grained reservoir. So far, the method
                      has been successfully applied to pure liquids. Coupling the
                      H-AdResS methodology to hybrid models of proteins, such as
                      the Molecular Mechanics/Coarse-Grained (MM/CG) scheme, is a
                      promising approach for rigorous calculations of ligand
                      binding free energies in low-resolution protein models.
                      Towards this goal, here we apply for the first time H-AdResS
                      to two atomistic proteins in dual-resolution solvent,
                      proving its ability to reproduce structural and dynamic
                      properties of both the proteins and the solvent, as obtained
                      from atomistic simulations.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {574 - Theory, modelling and simulation (POF3-574)},
      pid          = {G:(DE-HGF)POF3-574},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28992702},
      UT           = {WOS:000415911800041},
      doi          = {10.1021/acs.jctc.7b00508},
      url          = {https://juser.fz-juelich.de/record/838466},
}