N-[1-C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c |
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Authors: | Ronald A. Nieman Devens Gust John R. Cronin |
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Abstract: | The reaction of N-[1-13C] acetylimidazole with cytochrome c and guanidinated cytochrome c was evaluated as a means of introducing NMR-detectable groups as conformation-dependent probes. Resonances from both N-[1-13C]acetyl lysyl and O-[1-13C]acetyl tyrosyl groups were observed when ferricytochrome c was acetylated. However, only O-[1-13C]acetyl tyrosyl resonances were seen with acetylated guanidinated ferricytochrome c. Chemical shifts of the four O-[1-13C]acetyl tyrosyl groups were conformation dependent and ranged from 172 to 176 ppm. A convenient method for the preparation of N-[1-13C]acetylimidazole is described. |
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