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

Yi Tang, Giovanna Ghirlanda, Wendy A. Petka, Tadashi Nakajima, William F. DeGrado, David A. Tirrell

Research output: Contribution to journal › Article › peer-review

185 Scopus citations

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 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.

Original language	English (US)
Pages (from-to)	1494-1496
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	40
Issue number	8
DOIs	https://doi.org/10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X
State	Published - Apr 17 2001
Externally published	Yes

Keywords

Biosynthesis
Circular dichroism
Fluorine
Helical structures
Protein structures

ASJC Scopus subject areas

Catalysis
Chemistry(all)

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

Cite this

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title = "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 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.",

keywords = "Biosynthesis, Circular dichroism, Fluorine, Helical structures, Protein structures",

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year = "2001",

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

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T1 - Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability

AU - Tang, Yi

AU - Ghirlanda, Giovanna

AU - Petka, Wendy A.

AU - Nakajima, Tadashi

AU - DeGrado, William F.

AU - Tirrell, David A.

PY - 2001/4/17

Y1 - 2001/4/17

N2 - 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.

AB - 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.

KW - Biosynthesis

KW - Circular dichroism

KW - Fluorine

KW - Helical structures

KW - Protein structures

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

M3 - Article

AN - SCOPUS:0035901630

SN - 1433-7851

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 8

ER -

Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability

Abstract

Keywords

ASJC Scopus subject areas

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