title: NMR investigation of the copper(II)-carnosine complex in water solution.
abstract: The predominant species in water solution of excess carnosine and Cu2+ ions was characterized by measuring 13C and 1H spin-lattice and spin-spin relaxation rates. Four peptide molecules were calculated to be coordinated to the metal through the imidazole nitrogen. Evaluation of ion-proton distances demonstrated that metal complexation does not involve severe changes in conformation of the peptide.
authors.affiliation: Department of Chemistry, University of Siena, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Gaggelli
authors.forename: R
authors.initials: R
authors.lastname: Basosi
authors.forename: R
authors.initials: R
authors.lastname: Pogni
authors.forename: G
authors.initials: G
authors.lastname: Valensin
mesh_terms: D002336:Carnosine; D003300:Copper; D004151:Dipeptides; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D012996:Solutions
chemical_list: D004151:Dipeptides; D012996:Solutions; D003300:Copper; D002336:Carnosine