Qualitative aspects of hydrogen-deuterium exchange in the 1H, 13C, and 15N nuclear magnetic resonance spectra of viomycin in aqueous solution.
The 1H, 13C, and 15N high field nuclear magnetic resonance spectra of the cyclic peptide viomycin have been fully assigned using homo- and heteronuclear double resonance experiments and pH effects. In addition it is shown how the two- and three-bond H-D isotope effects upon carbonyl resonances may assist in their assignment. The resistance to exchange with solvent water of the amide proton involved in the transannular hydrogen bond is observed directly in the 1H spectra, via the isotope effect on a carbonyl resonance in the 13C spectra, and via the one-bond 1H couppling in the 15N spectra.
D002247:Carbon Isotopes; D003903:Deuterium; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D014756:Viomycin
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D003903:Deuterium; D014756:Viomycin