Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability

Yi Tang, Giovanna Ghirlanda, Wendy A. Petka, Tadashi Nakajima, William F. DeGrado, David A. Tirrell

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Fluorination of the hydrophobic core of a coiled-coil protein significantly improved its stability toward thermal and chemical denaturation. 5′,5′,5′-Trifluoroleucine (2) was efficiently incorporated into a leucinezipper protein in place of leucine (1) during E. coli biosynthesis. The fluorinated variant maintained stable secondary and tertiary structures under conditions that caused denaturation of the "wild-type" protein.

Original languageEnglish
Pages (from-to)1494-1496
Number of pages3
JournalAngewandte Chemie - International Edition
Issue number8
Publication statusPublished - Apr 17 2001



  • Biosynthesis
  • Circular dichroism
  • Fluorine
  • Helical structures
  • Protein structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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