Premium
Fluorinated Coiled‐Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability
Author(s) -
Tang Yi,
Ghirlanda Giovanna,
Petka Wendy A.,
Nakajima Tadashi,
DeGrado William F.,
Tirrell David A.
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010417)40:8<1494::aid-anie1494>3.0.co;2-x
Subject(s) - coiled coil , in vivo , thermal stability , materials science , electromagnetic coil , chemistry , biophysics , biochemistry , biology , engineering , organic chemistry , genetics , electrical engineering
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.