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Molecules 2017, 22(4), 655;

Protein Stability and Unfolding Following Glycine Radical Formation

Institute of Complex Systems: Structural Biochemistry (ICS-6) Forschungszentrum Jülich, 52425 Jülich, Germany
Institute of Chemistry, Faculty of Material Science, University of Miskolc, Egyetemváros 1, H-3529 Miskolc, Hungary
Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, Canada
Institute of Theoretical and Computational Chemistry, Heinrich Heine University Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany
Author to whom correspondence should be addressed.
Academic Editor: Roberta Galeazzi
Received: 15 March 2017 / Revised: 12 April 2017 / Accepted: 13 April 2017 / Published: 19 April 2017
(This article belongs to the Special Issue Biomolecular Simulations)
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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. View Full-Text
Keywords: protein oxidation; Trp cage; Trp zipper; villin headpiece; oxidative stress; molecular dynamics simulations protein oxidation; Trp cage; Trp zipper; villin headpiece; oxidative stress; molecular dynamics simulations

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Owen,, M.C.; Csizmadia, I.G.; Viskolcz, B.; Strodel, B. Protein Stability and Unfolding Following Glycine Radical Formation. Molecules 2017, 22, 655.

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