Loading...
Loading...

Go to the content (press return)

Atomic scale insights into urea–peptide interactions in solution

Author
Steinke, N.; Gillams, R.; Pardo, L.; Lorenz, C.; McLain, S.
Type of activity
Journal article
Journal
Physical chemistry chemical physics
Date of publication
2016-02-07
Volume
18
Number
5
First page
3862
Last page
3870
DOI
https://doi.org/10.1039/c5cp06646h Open in new window
Repository
http://hdl.handle.net/2117/103855 Open in new window
URL
https://apps-webofknowledge-com.recursos.biblioteca.upc.edu/full_record.do?product=WOS&search_mode=GeneralSearch&qid=8&SID=3B82rjNOqGmtIAHfAnr&page=1&doc=1 Open in new window
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 simu...
Citation
Steinke, N., Gillams, R., Pardo, L., Lorenz, C., McLain, S. Atomic scale insights into urea–peptide interactions in solution. "Physical chemistry chemical physics", 7 Febrer 2016, vol. 18, núm. 5, p. 3862-3870.
Keywords
AQUEOUS-SOLUTION, HYDRATION, INDUCED PROTEIN DENATURATION, LIQUID WATER, MOLECULAR-DYNAMICS, NEUTRON-DIFFRACTION EXPERIMENTS, PARTICLE MESH EWALD, POTENTIALS, SCATTERING, WATER-STRUCTURE
Group of research
CRnE - Barcelona Research Center in Multiscale Science and Engineering
GCM - Group of Characterization of Materials

Participants

  • Steinke, Nicola  (author)
  • Gillams, Richard J.  (author)
  • Pardo Soto, Luis Carlos  (author)
  • Lorenz, Christian D.  (author)
  • McLain, Sylvia E.  (author)

Attachments