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Structural studies of eukaryotic cytochrome c modified at methionine-65.


ABSTRACT: 1H n.m.r. spectra were recorded in both oxidation states for the following species: tuna cytochrome c, tuna [carboxymethylmethionine-65]cytochrome c, horse cytochrome c and horse [homoserine-65]cytochrome c. The experiments give the assignments of the singlet methyl resonances of methionine-65 and the N-terminal acetyl group. The modification at methionine-65 is shown to cause an extremely small structural perturbation to one part of the molecule close to the site of modification.

SUBMITTER: Boswell AP 

PROVIDER: S-EPMC1162631 | biostudies-other | 1981 Feb

REPOSITORIES: biostudies-other

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