Protein stability and unfolding following glycine radical formation

Michael C. Owen, Imre G. Csizmadia, Béla Viskolcz, Birgit Strodel

Research output: Contribution to journalArticle

3 Citations (Scopus)


Glycine (Gly) residues are particularly susceptible to hydrogen abstraction; which results in the formation of the capto-dative stabilized C-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 s. These results provide new evidence on the destabilizing effects of protein oxidation by reactive oxygen species.

Original languageEnglish
Article number655
Issue number4
Publication statusPublished - Apr 19 2017


  • Molecular dynamics simulations
  • Oxidative stress
  • Protein oxidation
  • Trp cage
  • Trp zipper
  • Villin headpiece

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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