Protein Stability and Unfolding Following Glycine Radical Formation
AbstractGlycine (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. View Full-Text
- Supplementary File 1:
PDF-Document (PDF, 530 KB)
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Owen,, M.C.; Csizmadia, I.G.; Viskolcz, B.; Strodel, B. Protein Stability and Unfolding Following Glycine Radical Formation. Molecules 2017, 22, 655.
Owen, MC, Csizmadia IG, Viskolcz B, Strodel B. Protein Stability and Unfolding Following Glycine Radical Formation. Molecules. 2017; 22(4):655.Chicago/Turabian Style
Owen,, Michael C.; Csizmadia, Imre G.; Viskolcz, Béla; Strodel, Birgit. 2017. "Protein Stability and Unfolding Following Glycine Radical Formation." Molecules 22, no. 4: 655.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.