Nuclear-magnetic-resonance studies of eukaryotic cytochrome c. Assignment of resonances of aromatic amino acids.
The aromatic 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. 33 resonances arising from 39 aroumatic protons of ferrocytochrome c, and 18 resonances arising from 27 aromatic protons of ferricytochrome c have been assigned.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D003574:Cytochrome c Group; D005399:Fishes; D006639:Histidine / Q000032:analysis; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D010649:Phenylalanine / Q000032:analysis; D011487:Protein Conformation; D011817:Rabbits; D013045:Species Specificity; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis
D000596:Amino Acids; D003574:Cytochrome c Group; D014443:Tyrosine; D010649:Phenylalanine; D006639:Histidine; D014364:Tryptophan