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

doi:10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X

Fluorinated Coiled-Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability

Angew Chem Int Ed Engl. 2001 Apr 17;40(8):1494-1496. doi: 10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X.

Authors

Yi Tang¹, Giovanna Ghirlanda², Wendy A Petka³, Tadashi Nakajima³, William F DeGrado², David A Tirrell¹

Affiliations

¹ Division of Chemistry and Chemical Engineering California Institute of Technology Pasadena, CA 91125 (USA) Fax: (+1) 626-793-8472.
² Department of Biochemistry & Biophysics University of Pennsylvania Philadelphia, PA 19104 (USA).
³ Department of Polymer Science and Engineering University of Massachusetts Amherst, MA 01003 (USA).

PMID: 29712367
DOI: 10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X

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 leucine-zipper 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.

Keywords: biosynthesis; circular dichroism; fluorine; helical structures; protein structures.