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Nat Methods. 2012 Oct;9(10):981-4. doi: 10.1038/nmeth.2175. Epub 2012 Sep 16.

Reversible labeling of native and fusion-protein motifs.

Author information

1
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California, USA.

Abstract

The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of Escherichia coli acyl carrier protein for visualization and functional studies. We use this iterative enzymatic methodology in vitro to reversibly label acyl carrier protein variants and apply these tools to NMR structural studies of protein-substrate interactions.

PMID:
22983458
PMCID:
PMC4128096
DOI:
10.1038/nmeth.2175
[Indexed for MEDLINE]
Free PMC Article

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