Nuclear-magnetic-resonance studies of eukaryotic cytochrome c. Assignment of resonances of aliphatic amino acids.
The aliphatic regions of the nuclear magnetic resonance spectra of horse ferricytochrome c and horse ferrocytochrome c are described. Resonance assignments have been made using NMR double-resonance techniques, spectral comparison of related proteins, the perturbing effects of extrinsic probes, and from knowledge of the X-ray structure of cytochrome c. There are eight firmly assigned methyl resonances of ferrocytochrome c and seven firmly assigned methyl resonances of ferricytochrome c.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D003574:Cytochrome c Group; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013045:Species Specificity
D000596:Amino Acids; D003574:Cytochrome c Group