Selective labeling of proteins by using protein farnesyltransferase

Benjamin P. Duckworth, Zhiyuan Zhang, Ayako Hosokawa, Mark D Distefano

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


The challenging task of identifying and studying protein function has been greatly aided by labeling proteins with reporter groups. Here, we present a strategy that utilizes an enzyme that labels a four-residue sequence appended onto the C terminus of a protein, with an alkyne-containing substrate. By using a bio-orthogonal cycloaddition reaction, a fluorophore that carried an azide moiety was then covalently coupled to the alkyne appended on the protein. FRET was used to calculate a Förster (R) distance of 40 Å between the eGFP chromophore and the newly appended Texas Red fluorophore. This experimental value is in good agreement with the predicted R value determined by using molecular modeling. The small recognition tag, the high specificity of the enzyme, and the orthogonal nature of the derivatization reaction will make this approach highly useful in protein chemistry.

Original languageEnglish (US)
Pages (from-to)98-105
Number of pages8
Issue number1
StatePublished - Jan 1 2007


  • Click chemistry
  • FRET
  • Protein farnesyltransferase
  • Protein immobilization
  • Protein modifications

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