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.
|Number of pages||3|
|Journal||Angewandte Chemie - International Edition|
|Publication status||Published - Apr 17 2001|
- Circular dichroism
- Helical structures
- Protein structures
ASJC Scopus subject areas