Simple and inexpensive incorporation of 19F-Tryptophan for protein NMR spectroscopy

被引：116

作者：

Crowley, Peter B. ^{[1
]}

Kyne, Ciara ^{[1
]}

Monteith, William B. ^{[1
]}

机构：

[1] Natl Univ Ireland Galway, Sch Chem, Galway, Ireland

来源：

CHEMICAL COMMUNICATIONS | 2012年 / 48卷 / 86期

基金：

爱尔兰科学基金会;

关键词：

GREEN FLUORESCENT PROTEIN; F-19; NMR; ESCHERICHIA-COLI; AMINO-ACIDS; TRYPTOPHAN SYNTHASE; GENETIC-CODE; DOMAIN; STATE; STABILITY; H-1-NMR;

D O I：

10.1039/c2cc35347d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Fluorine-containing amino acids are valuable probes for the biophysical characterization of proteins. Current methods for F-19-labeled protein production involve time-consuming genetic manipulation, compromised expression systems and expensive reagents. We show that Escherichia coli BL21, the workhorse of protein production, can utilise fluoroindole for the biosynthesis of proteins containing F-19-tryptophan.

引用

页码：10681 / 10683

页数：3

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