Issue 5, 2016

Atomic scale insights into urea–peptide interactions in solution


The mechanism by which proteins are denatured by urea is still not well understood, especially on the atomic scale where these interactions occur in vivo. In this study, the structure of the peptide GPG has been investigated in aqueous urea solutions in order to understand the combination of roles that both urea and water play in protein unfolding. Using a combination of neutron diffraction enhanced by isotopic substitution and computer simulations, it was found, in opposition with previous simulations studies, that urea is preferred over water around polar and charged portions of the peptides. Further, it appears that while urea directly replaces water around the nitrogen groups on GPG that urea and water occupy different positions around the peptide bond carbonyl groups. This suggests that urea may in fact weaken the peptide bond, disrupting the peptide backbone, thus ultimately causing denaturation.

Graphical abstract: Atomic scale insights into urea–peptide interactions in solution

Supplementary files

Article information

Article type
01 Nov 2015
06 Jan 2016
First published
07 Jan 2016
This article is Open Access
Creative Commons BY license

Phys. Chem. Chem. Phys., 2016,18, 3862-3870

Author version available

Atomic scale insights into urea–peptide interactions in solution

N. Steinke, R. J. Gillams, L. C. Pardo, C. D. Lorenz and S. E. McLain, Phys. Chem. Chem. Phys., 2016, 18, 3862 DOI: 10.1039/C5CP06646H

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