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Hydrogen bonds in the tripeptide Pro-Leu-Gly-NH2. 17O and 1H studies. 1984

H Gilboa, and A Steinschneider, and B Valentine, and D Dhawan, and D Fiat

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.

UI MeSH Term Description Entries
D009075 MSH Release-Inhibiting Hormone A hypothalamic tripeptide, enzymatic degradation product of OXYTOCIN, that inhibits the release of MELANOCYTE-STIMULATING HORMONES. MSH Release-Inhibiting Factor,Melanocyte-Stimulating Hormone Release-Inhibiting Hormone,Prolyl-Leucyl-Glycinamide,H-Pro-Leu-Gly-NH2,MIF-1,MIF-I,Melanocyte-Stimulating Hormone Release-Inhibiting Factor,Melanostatin,Oxytocin (7-9),Pro-Leu-Gly-NH2,Pro-Leu-Glyamide,Prol-Leu-Gly-NH2,Prolylleucylglycinamide,Prol Leu Gly NH2,Prolyl Leucyl Glycinamide
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D006860 Hydrogen Bonding A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond
D012997 Solvents Liquids that dissolve other substances (solutes), generally solids, without any change in chemical composition, as, water containing sugar. (Grant & Hackh's Chemical Dictionary, 5th ed) Solvent
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures

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