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Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
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 E. coli acyl carrier protein (ACP) for visualization and functio...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4128096/ https://www.ncbi.nlm.nih.gov/pubmed/22983458 http://dx.doi.org/10.1038/nmeth.2175 |
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author | Kosa, Nicolas M. Haushalter, Robert W. Smith, Andrew R. Burkart, Michael D. |
author_facet | Kosa, Nicolas M. Haushalter, Robert W. Smith, Andrew R. Burkart, Michael D. |
author_sort | Kosa, Nicolas M. |
collection | PubMed |
description | 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 E. coli acyl carrier protein (ACP) for visualization and functional studies. We utilize this iterative enzymatic methodology in vitro for reversible labeling variants and apply these tools to Nuclear Magnetic Resonance (NMR) structural studies of protein-substrate interactions. |
format | Online Article Text |
id | pubmed-4128096 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
record_format | MEDLINE/PubMed |
spelling | pubmed-41280962014-08-11 Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs Kosa, Nicolas M. Haushalter, Robert W. Smith, Andrew R. Burkart, Michael D. Nat Methods Article 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 E. coli acyl carrier protein (ACP) for visualization and functional studies. We utilize this iterative enzymatic methodology in vitro for reversible labeling variants and apply these tools to Nuclear Magnetic Resonance (NMR) structural studies of protein-substrate interactions. 2012-09-16 2012-10 /pmc/articles/PMC4128096/ /pubmed/22983458 http://dx.doi.org/10.1038/nmeth.2175 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Kosa, Nicolas M. Haushalter, Robert W. Smith, Andrew R. Burkart, Michael D. Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title | Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title_full | Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title_fullStr | Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title_full_unstemmed | Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title_short | Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs |
title_sort | reversible chemoenzymatic labeling of native and fusion carrier protein motifs |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4128096/ https://www.ncbi.nlm.nih.gov/pubmed/22983458 http://dx.doi.org/10.1038/nmeth.2175 |
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