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@ARTICLE{Owen:829362,
      author       = {Owen, Michael and Csizmadia, Imre G. and Viskolcz, Béla
                      and Strodel, Birgit},
      title        = {{P}rotein {S}tability and {U}nfolding {F}ollowing {G}lycine
                      {R}adical {F}ormation},
      journal      = {Molecules},
      volume       = {22},
      number       = {4},
      issn         = {1420-3049},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2017-03077},
      pages        = {655},
      year         = {2017},
      abstract     = {Glycine (Gly) residues are particularly susceptible to
                      hydrogen abstraction; which results in the formation of the
                      capto-dative stabilized Cα-centered Gly radical (GLR) on
                      the protein backbone. We examined the effect of GLR
                      formation on the structure of the Trp cage; tryptophan
                      zipper; and the villin headpiece; three fast-folding and
                      stable miniproteins; using all-atom (OPLS-AA) molecular
                      dynamics simulations. Radicalization changes the
                      conformation of the GLR residue and affects both neighboring
                      residues but did not affect the stability of the Trp zipper.
                      The stability of helices away from the radical center in
                      villin were also affected by radicalization; and GLR in
                      place of Gly15 caused the Trp cage to unfold within 1 µs.
                      These results provide new evidence on the destabilizing
                      effects of protein oxidation by reactive oxygen species.},
      cin          = {ICS-6},
      ddc          = {540},
      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:000404517800153},
      pubmed       = {pmid:28422069},
      doi          = {10.3390/molecules22040655},
      url          = {https://juser.fz-juelich.de/record/829362},
}