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Issue 86, 2012
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Simple and inexpensive incorporation of 19F-Tryptophan for protein NMR spectroscopy

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Abstract

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

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

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Publication details

The article was received on 24 Jul 2012, accepted on 10 Sep 2012 and first published on 24 Sep 2012


Article type: Communication
DOI: 10.1039/C2CC35347D
Citation: Chem. Commun., 2012,48, 10681-10683
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    Simple and inexpensive incorporation of 19F-Tryptophan for protein NMR spectroscopy

    P. B. Crowley, C. Kyne and W. B. Monteith, Chem. Commun., 2012, 48, 10681
    DOI: 10.1039/C2CC35347D

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