Issue 86, 2012

Simple and inexpensive incorporation of 19F-Tryptophan for proteinNMR spectroscopy

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

Supplementary files

Article information

Article type
Communication
Submitted
24 Jul 2012
Accepted
10 Sep 2012
First published
24 Sep 2012

Chem. Commun., 2012,48, 10681-10683

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements