Journal article icon

Journal article

Salt interactions in solution prevent direct association of urea with a peptide backbone

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 g...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

Actions


Access Document


Files:
Publisher copy:
10.1021/acs.jpcb.6b12542

Authors


More by this author
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Department:
St Peters College
Role:
Author
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:
1520-5207
ISSN:
1520-6106
Pubs id:
pubs:685951
URN:
uri:240805c0-8b32-4845-b111-dc2f1832dc85
UUID:
uuid:240805c0-8b32-4845-b111-dc2f1832dc85
Local pid:
pubs:685951
Paper number:
8
Language:
English

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP