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Updated: May 18, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Reversible labeling of native and fusion-protein motifs
Nicolas M Kosa1, Robert W Haushalter, Andrew R Smith
1Department 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.
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