Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

© 2018 Elsevier B.V. Molecular dynamics simulations were used to investigate the hydration and structure of the tripeptide GPG-NH2, and the effect of substituting a fluorine or hydroxyl group onto one of the Cαpositions in the glycinamide portion of the molecule. The fluorinated and hydroxylated peptides both display a slight dehydration of the proline and glycinamide residues and a different conformation of the glycinamide residue backbone than the GPG peptide. These two effects result in a significant decrease in the water-mediated interactions between the Gly1 and glycinamide residues, which had previously been shown to nucleate beta turns in GPG-NH2.

Original publication

DOI

10.1016/j.cplett.2018.05.068

Type

Journal article

Journal

Chemical Physics Letters

Publication Date

16/08/2018

Volume

706

Pages

228 - 236