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.
| Original language | English |
|---|---|
| Pages (from-to) | 347-350 |
| Number of pages | 4 |
| Journal | Analytical Biochemistry |
| Volume | 120 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Mar 1 1982 |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Nieman, R. A., Gust, J. D., & Cronin, J. R. (1982). N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c. Analytical Biochemistry, 120(2), 347-350. https://doi.org/10.1016/0003-2697(82)90356-6