Published April 17, 2001
| public
Journal Article
Fluorinated Coiled-Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability
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.
Additional Information
Issue published online: 17 APR 2001. Article first published online: 17 APR 2001. Manuscript Received: 2 JAN 2001. This work was supported by a grant from the U.S. Army Research Office. Y. Tang is supported by a Whitaker Graduate Research Fellowship. We thank Dr. Gary Hathaway for performing matrix-assisted laser desorption/ionization analyses.Additional details
- Eprint ID
- 53958
- DOI
- 10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X
- Resolver ID
- CaltechAUTHORS:20150121-143801079
- Army Research Office (ARO)
- Whitaker Graduate Research Fellowship
- Created
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2015-01-21Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field