TY  - JOUR
AU  - Owen, Michael
AU  - Csizmadia, Imre G.
AU  - Viskolcz, Béla
AU  - Strodel, Birgit
TI  - Protein Stability and Unfolding Following Glycine Radical Formation
JO  - Molecules
VL  - 22
IS  - 4
SN  - 1420-3049
CY  - Basel
PB  - MDPI
M1  - FZJ-2017-03077
SP  - 655
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000404517800153
C6  - pmid:28422069
DO  - DOI:10.3390/molecules22040655
UR  - https://juser.fz-juelich.de/record/829362
ER  -