N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies

Acetylation of cytochrome c

Ronald A. Nieman, John Devens Gust, John R. Cronin

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2 Citations (Scopus)

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 languageEnglish
Pages (from-to)347-350
Number of pages4
JournalAnalytical Biochemistry
Volume120
Issue number2
DOIs
Publication statusPublished - Mar 1 1982

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Acetylation
Cytochromes c
Nuclear magnetic resonance
Conformations
Proteins
Chemical shift

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies : Acetylation of cytochrome c. / Nieman, Ronald A.; Gust, John Devens; Cronin, John R.

In: Analytical Biochemistry, Vol. 120, No. 2, 01.03.1982, p. 347-350.

Research output: Contribution to journalArticle

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