Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy

Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of sid...

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Autores principales:	Ruth B. Pritchard, D. Flemming Hansen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0da10a54a94e459fb2afae5adb60909a
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spelling	oai:doaj.org-article:0da10a54a94e459fb2afae5adb60909a2021-12-02T14:39:00ZCharacterising side chains in large proteins by protonless 13C-detected NMR spectroscopy10.1038/s41467-019-09743-42041-1723https://doaj.org/article/0da10a54a94e459fb2afae5adb60909a2019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09743-4https://doaj.org/toc/2041-1723Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of side-chain conformational dynamics of six different amino acid types in medium-to-large proteins.Ruth B. PritchardD. Flemming HansenNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ruth B. Pritchard D. Flemming Hansen Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
description	Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of side-chain conformational dynamics of six different amino acid types in medium-to-large proteins.
format	article
author	Ruth B. Pritchard D. Flemming Hansen
author_facet	Ruth B. Pritchard D. Flemming Hansen
author_sort	Ruth B. Pritchard
title	Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_short	Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_full	Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_fullStr	Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_full_unstemmed	Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_sort	characterising side chains in large proteins by protonless 13c-detected nmr spectroscopy
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/0da10a54a94e459fb2afae5adb60909a
work_keys_str_mv	AT ruthbpritchard characterisingsidechainsinlargeproteinsbyprotonless13cdetectednmrspectroscopy AT dflemminghansen characterisingsidechainsinlargeproteinsbyprotonless13cdetectednmrspectroscopy
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Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy

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