Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins

Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 re...

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Detalles Bibliográficos
Autores principales: Brewster, Richard C., Gavins, Georgina C., Günthardt, Barbara, Farr, Sarah, Webb, Kimberly M., Voigt, Philipp, Hulme, Alison N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2016
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5656099/
https://www.ncbi.nlm.nih.gov/pubmed/27722332
http://dx.doi.org/10.1039/c6cc06801d
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author Brewster, Richard C.
Gavins, Georgina C.
Günthardt, Barbara
Farr, Sarah
Webb, Kimberly M.
Voigt, Philipp
Hulme, Alison N.
author_facet Brewster, Richard C.
Gavins, Georgina C.
Günthardt, Barbara
Farr, Sarah
Webb, Kimberly M.
Voigt, Philipp
Hulme, Alison N.
author_sort Brewster, Richard C.
collection PubMed
description Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.
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spelling pubmed-56560992018-01-05 Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins Brewster, Richard C. Gavins, Georgina C. Günthardt, Barbara Farr, Sarah Webb, Kimberly M. Voigt, Philipp Hulme, Alison N. Chem Commun (Camb) Chemistry Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity. Royal Society of Chemistry 2016-10-21 2016-09-13 /pmc/articles/PMC5656099/ /pubmed/27722332 http://dx.doi.org/10.1039/c6cc06801d Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Brewster, Richard C.
Gavins, Georgina C.
Günthardt, Barbara
Farr, Sarah
Webb, Kimberly M.
Voigt, Philipp
Hulme, Alison N.
Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title_full Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title_fullStr Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title_full_unstemmed Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title_short Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
title_sort chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5656099/
https://www.ncbi.nlm.nih.gov/pubmed/27722332
http://dx.doi.org/10.1039/c6cc06801d
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