Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR

Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N(ε)–C(ζ) bond of arginine side chains. An application to a 19 kDa protein shows that the strengths of interactions involving...

Descripción completa

Detalles Bibliográficos
Autores principales: Gerecht, Karola, Figueiredo, Angelo Miguel, Hansen, D. Flemming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708338/
https://www.ncbi.nlm.nih.gov/pubmed/28840203
http://dx.doi.org/10.1039/c7cc04821a
_version_ 1783282629087330304
author Gerecht, Karola
Figueiredo, Angelo Miguel
Hansen, D. Flemming
author_facet Gerecht, Karola
Figueiredo, Angelo Miguel
Hansen, D. Flemming
author_sort Gerecht, Karola
collection PubMed
description Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N(ε)–C(ζ) bond of arginine side chains. An application to a 19 kDa protein shows that the strengths of interactions involving arginine side chains can be characterised.
format Online
Article
Text
id pubmed-5708338
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Royal Society of Chemistry
record_format MEDLINE/PubMed
spelling pubmed-57083382018-01-05 Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR Gerecht, Karola Figueiredo, Angelo Miguel Hansen, D. Flemming Chem Commun (Camb) Chemistry Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N(ε)–C(ζ) bond of arginine side chains. An application to a 19 kDa protein shows that the strengths of interactions involving arginine side chains can be characterised. Royal Society of Chemistry 2017-09-16 2017-08-25 /pmc/articles/PMC5708338/ /pubmed/28840203 http://dx.doi.org/10.1039/c7cc04821a Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Gerecht, Karola
Figueiredo, Angelo Miguel
Hansen, D. Flemming
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title_full Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title_fullStr Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title_full_unstemmed Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title_short Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR
title_sort determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected nmr
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708338/
https://www.ncbi.nlm.nih.gov/pubmed/28840203
http://dx.doi.org/10.1039/c7cc04821a
work_keys_str_mv AT gerechtkarola determiningrotationaldynamicsoftheguanidinogroupofargininesidechainsinproteinsbycarbondetectednmr
AT figueiredoangelomiguel determiningrotationaldynamicsoftheguanidinogroupofargininesidechainsinproteinsbycarbondetectednmr
AT hansendflemming determiningrotationaldynamicsoftheguanidinogroupofargininesidechainsinproteinsbycarbondetectednmr

Ejemplares similares