Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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 publication

DOI

10.1021/acs.jpcb.6b12542

Type

Journal article

Journal

J Phys Chem B

Publication Date

02/03/2017

Volume

121

Pages

1866 - 1876

Keywords

Hydrogen Bonding, Hydrogen-Ion Concentration, Molecular Dynamics Simulation, Neutron Diffraction, Oligopeptides, Osmolar Concentration, Protein Denaturation, Salts, Solutions, Trifluoroacetic Acid, Urea, X-Ray Diffraction