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- W2805489543 abstract "Abstract 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 Cα positions 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." @default.
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- W2805489543 date "2018-08-01" @default.
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- W2805489543 title "On the hydration structure of the pro-drug GPG-NH2 and its derivatives" @default.
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- W2805489543 doi "https://doi.org/10.1016/j.cplett.2018.05.068" @default.
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