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@ARTICLE{Diddens:845650,
      author       = {Diddens, Diddo and Lesch, Volker and Heuer, Andreas and
                      Smiatek, Jens},
      title        = {{A}queous ionic liquids and their influence on peptide
                      conformations: denaturation and dehydration mechanisms},
      journal      = {Physical chemistry, chemical physics},
      volume       = {19},
      number       = {31},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2018-02866},
      pages        = {20430 - 20440},
      year         = {2017},
      abstract     = {Low concentrated aqueous ionic liquids (ILs) and their
                      influence on protein structures have attracted a lot of
                      interest over the last few years. This can be mostly
                      attributed to the fact that aqueous ILs, depending on the
                      ion species involved, can be used as protein protectants or
                      protein denaturants. Atomistic molecular dynamics (MD)
                      simulations are performed in order to study the influence of
                      different aprotic ILs on the properties of a short hairpin
                      peptide. Our results reveal distinct binding and
                      denaturation effects for 1-ethyl-3-methylimidazolium (EMIM)
                      in combination with different anions, namely, chloride (CL),
                      tetrafluoroborate (BF4) and acetate (ACE). The simulation
                      outcomes demonstrate that the studied ILs with larger anions
                      reveal a more pronounced accumulation behavior of the
                      individual ion species around the peptide, which is
                      accomplished by a stronger dehydration effect. We can relate
                      these findings to the implications of the Kirkwood–Buff
                      theory, which provides a thermodynamic explanation for the
                      denaturation strength in terms of the IL accumulation
                      behavior. The results for the spatial distribution
                      functions, the binding energies and the local/bulk partition
                      coefficients are in good agreement with metadynamics
                      simulations in order to determine the energetically most
                      stable peptide conformations. The free energy landscapes
                      indicate a decrease of the denaturation strength in the
                      order EMIM/ACE, EMIM/BF4 and EMIM/CL, which coincides with a
                      decreasing size of the anion species. An analysis of the
                      potential binding energies reveals that this effect is
                      mainly of enthalpic nature.},
      cin          = {IEK-12},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IEK-12-20141217},
      pnm          = {131 - Electrochemical Storage (POF3-131)},
      pid          = {G:(DE-HGF)POF3-131},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28737791},
      UT           = {WOS:000407763700012},
      doi          = {10.1039/C7CP02897K},
      url          = {https://juser.fz-juelich.de/record/845650},
}