Issue 4, 2008
From the journal:

Chemical Communications

Site-specific N-terminal labelling of proteinsin vitro and in vivo using N-myristoyl transferase and bioorthogonal ligation chemistry†

William P. Heal,a   Sasala R. Wickramasinghe,a   Paul W. Bowyer,‡a   Anthony A. Holder,b   Deborah F. Smith,c   Robin J. Leatherbarrow*a  and  Edward W. Tate*a  

* Corresponding authors

a Department of Chemistry, South Kensington Campus, Imperial College, London, UK
E-mail: e.tate@ic.ac.uk, r.leatherbarrow@ic.ac.uk
Fax: +44 (0)20 75941139
Tel: +44 (0)20 75943752

b Division of Parasitology, MRC National Institute for Medical Research, Mill Hill, London, UK

c Immunology and Infection Unit, Department of Biology, University of York, UK

Abstract

N-Myristoyl transferase-mediated modification with azide-bearing substrates is introduced as a highly selective and practical method for in vitro and in vivo N-terminal labelling of a recombinant protein using bioorthogonal ligation chemistry.

Graphical abstract: Site-specific N-terminal labelling of proteinsin vitro and in vivo using N-myristoyl transferase and bioorthogonal ligation chemistry

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Article information

DOI
https://doi.org/10.1039/B716115H
Article type
Communication
Submitted
18 Oct 2007
Accepted
05 Nov 2007
First published
13 Nov 2007

Chem. Commun., 2008, 480-482

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Site-specific N-terminal labelling of proteinsin vitro and in vivo using N-myristoyl transferase and bioorthogonal ligation chemistry

W. P. Heal, S. R. Wickramasinghe, P. W. Bowyer, A. A. Holder, D. F. Smith, R. J. Leatherbarrow and E. W. Tate, Chem. Commun., 2008, 480 DOI: 10.1039/B716115H

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