The stability of ferricytochrome c. Temperature dependence of its NMR spectrum.
The temperature dependence of the nuclear magnetic resonance spectrum of horse ferricytochrome c is described. The protein maintains an ordered structure over the temperature range 20 degrees C to 77 degrees C. The temperature dependence of the spectrum of ferricytochrome c arises from a number of causes including the paramagnetism of the ferric ion and protein structural changes. Preliminary analysis of the data show that the region of the protein about Ile-57 is flexible. Comparison of the data with the analogous data for horse ferrocytochrome c reveals that there is a small difference in structure between cytochrome c in its two oxidation states in the region about Ile-57.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003574:Cytochrome c Group; D004355:Drug Stability; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D013696:Temperature
D000596:Amino Acids; D003574:Cytochrome c Group