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@ARTICLE{CarballoPacheco:858906,
      author       = {Carballo-Pacheco, Martín and Ismail, Ahmed E. and Strodel,
                      Birgit},
      title        = {{O}n the {A}pplicability of {F}orce {F}ields {T}o {S}tudy
                      the {A}ggregation of {A}myloidogenic {P}eptides {U}sing
                      {M}olecular {D}ynamics {S}imulations},
      journal      = {Journal of chemical theory and computation},
      volume       = {14},
      number       = {11},
      issn         = {1549-9626},
      address      = {Washington, DC},
      reportid     = {FZJ-2018-07742},
      pages        = {6063 - 6075},
      year         = {2018},
      abstract     = {Molecular dynamics simulations play an essential role in
                      understanding biomolecular processes such as protein
                      aggregation at temporal and spatial resolutions which are
                      not attainable by experimental methods. For a correct
                      modeling of protein aggregation, force fields must
                      accurately represent molecular interactions. Here, we study
                      the effect of five different force fields on the oligomer
                      formation of Alzheimer’s Aβ16–22 peptide and two of its
                      mutants: Aβ16–22(F19V,F20V), which does not form fibrils,
                      and Aβ16–22(F19L) which forms fibrils faster than the
                      wild type. We observe that while oligomer formation kinetics
                      depends strongly on the force field, structural properties,
                      such as the most relevant protein–protein contacts, are
                      similar between them. The oligomer formation kinetics
                      obtained with different force fields differ more from each
                      other than the kinetics between aggregating and
                      nonaggregating peptides simulated with a single force field.
                      We discuss the difficulties in comparing atomistic
                      simulations of amyloid oligomer formation with experimental
                      observables.},
      cin          = {ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30336669},
      UT           = {WOS:000450695200053},
      doi          = {10.1021/acs.jctc.8b00579},
      url          = {https://juser.fz-juelich.de/record/858906},
}