Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group

Woon Ki Lim, Jörg Rösgen, and S. Walter Englander
PNAS February 24, 2009 106 (8) 2595-2600; https://doi.org/10.1073/pnas.0812588106

  1. Contributed by S. Walter Englander, December 10, 2008 (received for review November 25, 2008)

Abstract

The mechanism by which urea and guanidinium destabilize protein structure is controversial. We tested the possibility that these denaturants form hydrogen bonds with peptide groups by measuring their ability to block acid- and base-catalyzed peptide hydrogen exchange. The peptide hydrogen bonding found appears sufficient to explain the thermodynamic denaturing effect of urea. Results for guanidinium, however, are contrary to the expectation that it might H-bond. Evidently, urea and guanidinium, although structurally similar, denature proteins by different mechanisms.

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Footnotes

  • 1To whom correspondence may be addressed. E-mail: jorosgen{at}utmb.edu or engl{at}mail.med.upenn.edu

  • Author contributions: W.K.L., J.R., and S.W.E. designed research; W.K.L. performed research; W.K.L. and J.R. analyzed data; and J.R. and S.W.E. wrote the paper.

  • The authors declare no conflict of interest.

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Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
Woon Ki Lim, Jörg Rösgen, S. Walter Englander
Proceedings of the National Academy of Sciences Feb 2009, 106 (8) 2595-2600; DOI: 10.1073/pnas.0812588106
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