Journal article
Salt interactions in solution prevent direct association of urea with a peptide backbone
- Abstract:
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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 g...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Accepted manuscript, pdf, 8.8MB)
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- Publisher copy:
- 10.1021/acs.jpcb.6b12542
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Authors
Funding
Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Journal of Physical Chemistry B Journal website
- Volume:
- 121
- Issue:
- 8
- Pages:
- 1866-1876
- Publication date:
- 2017-03-02
- Acceptance date:
- 2017-01-30
- DOI:
- EISSN:
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1520-5207
- ISSN:
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1520-6106
- Source identifiers:
-
685951
Item Description
- Language:
- English
- Pubs id:
-
pubs:685951
- UUID:
-
uuid:240805c0-8b32-4845-b111-dc2f1832dc85
- Local pid:
- pubs:685951
- Deposit date:
- 2017-03-15
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2017
- Notes:
- Copyright © 2017 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from the American Chemical Society at: https://doi.org/10.1021/acs.jpcb.6b12542
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