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

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

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
Volume40
Issue number8
DOIs
Publication statusPublished - Apr 17 2001

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Chemical stability
Denaturation
Thermodynamic stability
Display devices
Proteins
Fluorination
Biosynthesis
Leucine
Escherichia coli

Keywords

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

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability. / Tang, Yi; Ghirlanda, Giovanna; Petka, Wendy A.; Nakajima, Tadashi; DeGrado, William F.; Tirrell, David A.

In: Angewandte Chemie - International Edition, Vol. 40, No. 8, 17.04.2001, p. 1494-1496.

Research output: Contribution to journalArticle

Tang, Yi ; Ghirlanda, Giovanna ; Petka, Wendy A. ; Nakajima, Tadashi ; DeGrado, William F. ; Tirrell, David A. / Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability. In: Angewandte Chemie - International Edition. 2001 ; Vol. 40, No. 8. pp. 1494-1496.
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