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Effect of urea on peptide conformation in water: Molecular dynamics and experimental characterization
Södertörn University, School of Life Sciences.
Södertörn University, School of Life Sciences. Karolinska Institutet.ORCID iD: 0000-0002-3049-967X
2005 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 89, no 2, 842-857 p.Article in journal (Refereed) Published
Abstract [en]

Molecular dynamics simulations of a ribonuclease A C-peptide analog and a sequence variant were performed in water at 277 and 300 K and in 8 M urea to clarify the molecular denaturation mechanism induced by urea and the early events in protein unfolding. Spectroscopic characterization of the peptides showed that the C-peptide analog had a high alpha-helical content, which was not the case for the variant. In the simulations, interdependent side-chain interactions were responsible for the high stability of the alpha-helical C-peptide analog in the different solvents. The other peptide displayed alpha-helical unwinding that propagated cooperatively toward the N-terminal. The conformations sampled by the peptides depended on their sequence and on the solvent. The ability of water molecules to form hydrogen bonds to the peptide as well as the hydrogen bond lifetimes increased in the presence of urea, whereas water mobility was reduced near the peptide. Urea accumulated in excess around the peptide, to which it formed long-lived hydrogen bonds. The unfolding mechanisms induced by thermal denaturation and by urea are of a different nature, with urea-aqueous solutions providing a better peptide solvation than pure water. Our results suggest that the effect of urea on the chemical denaturation process involves both the direct and indirect mechanisms.

Place, publisher, year, edition, pages
2005. Vol. 89, no 2, 842-857 p.
National Category
URN: urn:nbn:se:sh:diva-14449DOI: 10.1529/biophysj.105.061978ISI: 000230822200010PubMedID: 15908578ScopusID: 2-s2.0-23244452958OAI: diva2:480521
Available from: 2012-01-19 Created: 2011-12-23 Last updated: 2016-01-08Bibliographically approved

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Berndt, Kurt D
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