The solution structures of tuna and horse cytochromes c.
The nuclear magnetic resonance spectra of tuna ferricytochrome c and tuna ferrocytochrome c are described. Resonance assignments are made using NMR double-resonance techniques. A comparison of the NMR data for tuna cytochrome c with the previously reported data for horse cytochrome c shows that the proteins have virtually identical main-chain folds. Three regions of local conformational differences have been distinguished.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003574:Cytochrome c Group; D005399:Fishes; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012996:Solutions; D013045:Species Specificity
D000596:Amino Acids; D003574:Cytochrome c Group; D012996:Solutions