Solution structure of mitochondrial cytochrome c. I. 1H nuclear magnetic resonance of ferricytochrome c.
The 1H nuclear magnetic resonance spectra of tuna and horse ferricytochromes c have been investigated and the resonances of all amino acid methyl groups have been assigned to specific absorption lines. The assignment procedure involves principally the comparison of one-dimensional nuclear magnetic resonance spectra from a range of homologous ferricytochromes c and does not require a prior knowledge of the secondary or tertiary protein structure. Of the 49 methyl groups of tuna cytochrome c, the assignment of 33 is made without reference to the X-ray crystal structure. The method should therefore be applicable to other proteins of similar size where X-ray structures are unavailable. The assignments will be used to investigate the structure of cytochrome c in solution.
Williams
G
G
Moore
G R
GR
Porteous
R
R
Robinson
M N
MN
Soffe
N
N
Williams
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D002175:Candida; D010856:Columbidae; D003574:Cytochrome c Group; D006736:Horses; D007798:Lampreys; D007614:Macropodidae; D009682:Magnetic Resonance Spectroscopy; D008928:Mitochondria / Q000032:analysis*; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae; D012996:Solutions; D014413:Tuna
D003574:Cytochrome c Group; D012996:Solutions