Nuclear‐Magnetic‐Resonance Studies of Ferrocytochrome c
Open Access
- 1 February 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 103 (3), 513-521
- https://doi.org/10.1111/j.1432-1033.1980.tb05975.x
Abstract
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 °C and over the temperature range 4°C to 97 °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 upheld. 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.This publication has 36 references indexed in Scilit:
- Nuclear‐Magnetic‐Resonance Studies of Eukaryotic Cytochrome cEuropean Journal of Biochemistry, 1980
- Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome CFEBS Letters, 1976
- Conformational mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residuesFEBS Letters, 1976
- Assignment of aromatic amino acid PMR resonances of horse ferrocytochrome CFEBS Letters, 1975
- Assignment of aromatic amino acid PMR resonances of horse ferricytochrome cFEBS Letters, 1975
- Structural studies by proton NMR of cytochrome c‐557 from Crithidia oncopeltiFEBS Letters, 1973
- Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome cJournal of Molecular Biology, 1973
- Some aspects of pH and temperature dependence of the NMR spectra of cytochrome cBiochemical and Biophysical Research Communications, 1971
- Proton magnetic resonance evidence for methionine-iron coordination in mammalian-type ferrocytochrome cBiochemical and Biophysical Research Communications, 1969
- Studies on Cytochrome c. I. Electrophoretic Purification of Cytochrome c and its Amino Acid Composition*Journal of the American Chemical Society, 1941