Salt Interactions in Solution Prevent Direct Association of Urea with a Peptide Backbone

Nicola Steinke, Anna Genina, Christian D Lorenz, Sylvia E. McLain

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)
239 Downloads (Pure)

Abstract

There is an ongoing debate as to how urea denatures proteins in solution. Using a combination of neutron scattering and computer simulation of a model peptide KGPGK, it was found that the ionic strength and pH have a significant impact on the urea-peptide interaction. From the work presented here, it appears that urea first and foremost decreases the charge-based interactions in solution, such as the TFA-TFA association, before interacting with the peptide backbone via hydrogen bonds. This gives insight into the pH and salt concentration dependency of urea-caused protein denaturation and might unify direct and indirect theories of urea-induced protein denaturation. The observed differences between MD and neutron and X-ray diffraction data might show that MD, in this particular case, underestimates the influence of charged fluorinated solutes.

Original languageEnglish
Pages (from-to)1866-1876
Number of pages11
JournalThe Journal of Physical Chemistry B
Volume121
Issue number8
Early online date30 Jan 2017
DOIs
Publication statusPublished - 2 Mar 2017

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