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• W4238683672 abstract "Removing phosphopantetheine-tagged labels from acyl carrier proteins (ACPs) and ACP fusion proteins contributes to a versatile labeling method in which tags can be iteratively swapped. 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." @default.
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• W4238683672 date "2012-09-16" @default.
• W4238683672 modified "2023-09-27" @default.
• W4238683672 title "Reversible labeling of native and fusion-protein motifs" @default.
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• W4238683672 doi "https://doi.org/10.1038/nmeth.2175" @default.
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