title: 17O, 14N and 15N n.m.r. studies of the Co2+ complexes of cyclo(Pro17O-Gly15N) and cyclo(Gly17O-Pro) in aqueous solution.
abstract: The complexation of cyclo(Pro17O-Gly15N) and cyclo(Gly17O-Pro) with Co2+ ions has been studied by 17O, 14N and 15N n.m.r. spectroscopy in aqueous solution. 17O, 14N and 15N transverse relaxation times and chemical shifts were measured as a function of temperature. The 17O n.m.r. studies unequivocally demonstrate that the cobaltous ion binds to the peptide oxygen of both compounds. The hyperfine coupling constant and the peptide residence times were found to be A = -0.165 MHz and -0.145 MHz, tau m = 16, and 92 microseconds for cyclo(Pro17O-Gly15N) and cyclo(Gly17O-Pro), respectively. The 14N and 15N studies of labeled cyclo(Pro17O-Gly15N) do not indicate binding at either the Gly15N or the Pro14N site.
authors.affiliation: Department of Physiology and Biophysics, University of Illinois, Chicago.
authors.forename: J
authors.initials: J
authors.lastname: Tritt-Goc
authors.forename: R
authors.initials: R
authors.lastname: Goc
authors.forename: E
authors.initials: E
authors.lastname: Ponnusamy
authors.forename: D
authors.initials: D
authors.lastname: Fiat
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003035:Cobalt / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D009587:Nitrogen Isotopes; D010103:Oxygen Isotopes; D010456:Peptides, Cyclic / Q000032:analysis / Q000138:chemical synthesis*; D012996:Solutions; D013696:Temperature; D013816:Thermodynamics
chemical_list: D009587:Nitrogen Isotopes; D010103:Oxygen Isotopes; D010456:Peptides, Cyclic; D012996:Solutions; C016325:cyclo(glycylprolyl); D003035:Cobalt; C062238:cyclo(prolylglycyl)