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Atomic scale insights into urea-peptide interactions in solution

Atomic scale insights into urea-peptide interactions in solution
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.

1463-9076
3862-3870
Steinke, Nicola
c5b12ef5-f763-4b40-872c-794e841599ed
Gillams, Richard J.
89341fe4-db94-4d27-a5be-c092e2e8de5b
Pardo, Luis Carlos
f73562ac-2cbc-4a2c-8352-765cd05691cc
Lorenz, Christian D.
080b1193-25c1-49da-968a-ef522fdbec59
McLain, Sylvia E.
f0b6c048-e499-4eca-801e-359ac928f502
Steinke, Nicola
c5b12ef5-f763-4b40-872c-794e841599ed
Gillams, Richard J.
89341fe4-db94-4d27-a5be-c092e2e8de5b
Pardo, Luis Carlos
f73562ac-2cbc-4a2c-8352-765cd05691cc
Lorenz, Christian D.
080b1193-25c1-49da-968a-ef522fdbec59
McLain, Sylvia E.
f0b6c048-e499-4eca-801e-359ac928f502

Steinke, Nicola, Gillams, Richard J., Pardo, Luis Carlos, Lorenz, Christian D. and McLain, Sylvia E. (2016) Atomic scale insights into urea-peptide interactions in solution. Physical Chemistry Chemical Physics, 18 (5), 3862-3870. (doi:10.1039/c5cp06646h).

Record type: Article

Abstract

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.

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Accepted/In Press date: 6 January 2016
e-pub ahead of print date: 7 January 2016

Identifiers

Local EPrints ID: 434258
URI: http://eprints.soton.ac.uk/id/eprint/434258
ISSN: 1463-9076
PURE UUID: 6ff6bba8-d76c-44fc-92ff-3f93447f7da3
ORCID for Richard J. Gillams: ORCID iD orcid.org/0000-0002-8597-8723

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Date deposited: 18 Sep 2019 16:30
Last modified: 07 Oct 2020 02:15

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Contributors

Author: Nicola Steinke
Author: Richard J. Gillams ORCID iD
Author: Luis Carlos Pardo
Author: Christian D. Lorenz
Author: Sylvia E. McLain

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