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@ARTICLE{Irbck:8935,
      author       = {Irbäck, A. and Mitternacht, S. and Mohanty, S.},
      title        = {{A}n effective all-­atom potential for proteins},
      journal      = {PMC Biophysics},
      volume       = {2},
      issn         = {1757-5036},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-8935},
      pages        = {2},
      year         = {2009},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We describe and test an implicit solvent all-atom potential
                      for simulations of protein folding and aggregation. The
                      potential is developed through studies of structural and
                      thermodynamic properties of 17 peptides with diverse
                      secondary structure. Results obtained using the final form
                      of the potential are presented for all these peptides. The
                      same model, with unchanged parameters, is furthermore
                      applied to a heterodimeric coiled-coil system, a mixed
                      alpha/beta protein and a three-helix-bundle protein, with
                      very good results. The computational efficiency of the
                      potential makes it possible to investigate the free-energy
                      landscape of these 49-67-residue systems with high
                      statistical accuracy, using only modest computational
                      resources by today's standards.PACS Codes: 87.14.E-,
                      87.15.A-, 87.15.Cc.},
      cin          = {JSC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JSC-20090406},
      pnm          = {Scientific Computing},
      pid          = {G:(DE-Juel1)FUEK411},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19356242},
      pmc          = {pmc:PMC2696411},
      doi          = {10.1186/1757-5036-2-2},
      url          = {https://juser.fz-juelich.de/record/8935},
}