CaltechAUTHORS
Published April 17, 2001 | Version public
Journal Article Metadata-only

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

Creators

  • 1. ROR icon California Institute of Technology
  • 2. ROR icon University of Pennsylvania
  • 3. ROR icon University of Massachusetts Amherst

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

Identifiers

Eprint ID
53958
DOI
10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X
Resolver ID
CaltechAUTHORS:20150121-143801079

Related works

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

Funding

Army Research Office (ARO)
Whitaker Graduate Research Fellowship

Dates

Created
2015-01-21
Created from EPrint's datestamp field
Updated
2021-11-10
Created from EPrint's last_modified field