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@ARTICLE{Owen:823866,
      author       = {Owen, Michael C. and Strodel, Birgit and Csizmadia, Imre G.
                      and Viskolcz, Béla},
      title        = {{R}adical {F}ormation {I}nitiates {S}olvent-{D}ependent
                      {U}nfolding and β-{S}heet {F}ormation in a {M}odel
                      {H}elical {P}eptide},
      journal      = {The journal of physical chemistry / B},
      volume       = {120},
      number       = {22},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2016-06506},
      pages        = {4878 - 4889},
      year         = {2016},
      abstract     = {We examined the effects of Cα-centered radical formation
                      on the stability of a model helical peptide,
                      N-Ac-KK(AL)10KK-NH2. Three, 100 ns molecular dynamics
                      simulations using the OPLS-AA force field were carried out
                      on each α-helical peptide in six distinct binary TIP4P
                      water/2,2,2-trifluoroethanol (TFE) mixtures. The α-helicity
                      was at a maximum in $20\%$ TFE, which was inversely
                      proportional to the number of H-bonds between water
                      molecules and the peptide backbone. The radial distribution
                      of TFE around the peptide backbone was highest in $20\%$
                      TFE, which enhanced helix stability. The Cα-centered
                      radical initiated the formation of a turn within 5 ns, which
                      was a smaller kink at high TFE concentrations, and a loop at
                      lower TFE concentrations. The highest helicity of the
                      peptide radical was measured in $100\%$ TFE. The formation
                      of hydrogen bonds between the peptide backbone and water
                      destabilized the helix, whereas the clustering of TFE
                      molecules around the radical center stabilized the helix.
                      Following radical termination, the once helical structure
                      converted to a β-sheet rich state in $100\%$ water only,
                      and this transition did not occur in the nonradical control
                      peptide. This study gives evidence on how the formation of
                      peptide radicals can initiate α-helical to β-sheet
                      transitions under oxidative stress conditions.},
      cin          = {ICS-6},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000377841200002},
      pubmed       = {pmid:27169334},
      doi          = {10.1021/acs.jpcb.6b00174},
      url          = {https://juser.fz-juelich.de/record/823866},
}