Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence.
The pH dependence and the temperature dependence of the nuclear magnetic resonance spectrum of horse ferrocytochrome c are described. This protein is very stable; it maintains an ordered structure over the pH range 4 to 12 at 25 degrees C and over the temperature range 4 degrees C to 97 degrees C at pH 7.0. The dynamic characteristics of the conformation of ferrocytochrome c were investigated. Particular emphasis was laid on the aromatic resonances and resonances of methyl groups shifted far upfield. Tyr-48 and Phe-46 were found to be relatively immobile whilst a region of the protein close to Ile-57 was found to be relatively flexible.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003574:Cytochrome c Group; D004355:Drug Stability; D006736:Horses; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013696:Temperature
D000596:Amino Acids; D003574:Cytochrome c Group