1H- and 13C-N.M.R. spectra of eledoisin and intermediate oligopeptides.
The 1H- and 13C-n.m.r. spectra of eledoisin and minor oligopeptides were measured and assigned. The proton spectra were interpreted on the basis of homonuclear decoupling, chemical shift criteria and spectra simulation. The information obtained was used in the assignment of the 13C spectrum via heteronuclear 1H-13C. The steric arrangement of proline residue was deduced from the 13C spectrum. Moreover the similarity of the 13C spectrum of eledoisin with that of component oligopeptides suggests that no considerable conformational change occurs in the undecapeptide relative to the component fragments.
D002247:Carbon Isotopes; D055598:Chemical Phenomena; D002621:Chemistry; D004600:Eledoisin; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D010446:Peptide Fragments; D011392:Proline / Q000032:analysis; D011487:Protein Conformation
D002247:Carbon Isotopes; D009842:Oligopeptides; D010446:Peptide Fragments; D004600:Eledoisin; D006859:Hydrogen; D011392:Proline