Chemical Communications 2012-11-07

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

Peter B Crowley, Ciara Kyne, William B Monteith

Index: Chem. Commun. (Camb.) 48(86) , 10681-3, (2012)

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Abstract

Fluorine-containing amino acids are valuable probes for the biophysical characterization of proteins. Current methods for (19)F-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 (19)F-tryptophan.