Hydrogen bonds in the tripeptide Pro-Leu-Gly-NH2. 17O and 1H studies.
17O-NMR measurements of labeled Pro-Leu-Gly-NH2 were carried out at different pH levels and in mixed solvents of water/acetonitrile. Complementary studies of the amide protons were carried out in acetonitrile-d3. Only the prolyl C = 17O group was sensitive to the pH level. Protonation of the amine group resulted in an upfield chemical shift of 18 ppm. The chemical shifts of each of the three oxygen sites was sensitive to the ratio water:acetonitrile. Solvent composition dependence of the chemical shift and linewidth suggests that the prolyl C = 17O is involved in intramolecular hydrogen bond formation when Pro-Leu-Gly-NH2 is dissolved in acetonitrile, while in water there is no intramolecular H bond.
D006860:Hydrogen Bonding; D009075:MSH Release-Inhibiting Hormone; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D011487:Protein Conformation; D012997:Solvents; D013696:Temperature
D009842:Oligopeptides; D012997:Solvents; D009075:MSH Release-Inhibiting Hormone