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Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR

Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the paramagnetic labelling of proteins. The tag can be easily synthesized and is stereochemically homogenous over a wide range of temperatures, yielding NMR spectra with a single set of peaks. Bound to ubiquitin, it induced large resi...

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Autores principales: Peters, Fabian, Maestre-Martinez, Mitcheell, Leonov, Andrei, Kovačič, Lidija, Becker, Stefan, Boelens, Rolf, Griesinger, Christian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3193991/
https://www.ncbi.nlm.nih.gov/pubmed/21892794
http://dx.doi.org/10.1007/s10858-011-9560-y
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author Peters, Fabian
Maestre-Martinez, Mitcheell
Leonov, Andrei
Kovačič, Lidija
Becker, Stefan
Boelens, Rolf
Griesinger, Christian
author_facet Peters, Fabian
Maestre-Martinez, Mitcheell
Leonov, Andrei
Kovačič, Lidija
Becker, Stefan
Boelens, Rolf
Griesinger, Christian
author_sort Peters, Fabian
collection PubMed
description Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the paramagnetic labelling of proteins. The tag can be easily synthesized and is stereochemically homogenous over a wide range of temperatures, yielding NMR spectra with a single set of peaks. Bound to ubiquitin, it induced large residual dipolar couplings and pseudocontact shifts that could be measured easily and agreed very well with the protein structure. We show that Cys-Ph-TAHA can be used to label large proteins that are biochemically challenging such as the Lac repressor in a 90 kDa ternary complex with DNA and inducer. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10858-011-9560-y) contains supplementary material, which is available to authorized users.
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spelling pubmed-31939912011-11-07 Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR Peters, Fabian Maestre-Martinez, Mitcheell Leonov, Andrei Kovačič, Lidija Becker, Stefan Boelens, Rolf Griesinger, Christian J Biomol NMR Article Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the paramagnetic labelling of proteins. The tag can be easily synthesized and is stereochemically homogenous over a wide range of temperatures, yielding NMR spectra with a single set of peaks. Bound to ubiquitin, it induced large residual dipolar couplings and pseudocontact shifts that could be measured easily and agreed very well with the protein structure. We show that Cys-Ph-TAHA can be used to label large proteins that are biochemically challenging such as the Lac repressor in a 90 kDa ternary complex with DNA and inducer. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10858-011-9560-y) contains supplementary material, which is available to authorized users. Springer Netherlands 2011-09-04 2011 /pmc/articles/PMC3193991/ /pubmed/21892794 http://dx.doi.org/10.1007/s10858-011-9560-y Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Peters, Fabian
Maestre-Martinez, Mitcheell
Leonov, Andrei
Kovačič, Lidija
Becker, Stefan
Boelens, Rolf
Griesinger, Christian
Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title_full Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title_fullStr Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title_full_unstemmed Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title_short Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR
title_sort cys-ph-taha: a lanthanide binding tag for rdc and pcs enhanced protein nmr
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3193991/
https://www.ncbi.nlm.nih.gov/pubmed/21892794
http://dx.doi.org/10.1007/s10858-011-9560-y
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