title: 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
abstract: The CHn groups in the aliphatic side chains of horse cytochrome c have been characterized according to the chemical shifts of both 13C-NMR and 1H-NMR signals, their temperature dependence and the number of attached protons, n. The primary assignments of resonances from the 55 side-chain methyl and the 27 methine groups were obtained directly for the oxidised and the reduced forms. Specific assignments of the 13C resonances were obtained through shift-correlation experiments and comparison with earlier 1H-NMR studies, by further measurements of proton-proton interactions, or by elimination. Comparison of the paramagnetic shifts of carbon and protons indicates a small redox-related change of conformation in the vicinity of Trp59 and a significant expansion of the protein over 30-50 degrees C.
authors.affiliation: Centro de Tecnologia Química e Biológica, Oeiras, Portugal.
authors.forename: H
authors.initials: H
authors.lastname: Santos
authors.forename: D L
authors.initials: DL
authors.lastname: Turner
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003574:Cytochrome c Group / Q000737:chemistry*; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D013696:Temperature
chemical_list: D000596:Amino Acids; D003574:Cytochrome c Group