Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment

Structure determination of large proteins by solution state NMR is challenging due to spectral overlap. Here the authors present a labeling strategy using 2-13C and 3-13C pyruvate as carbon source for E. coli, which increases the effective resolution of triple-resonance HNCA experiments and helps to...

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Autores principales:	Scott A. Robson, Koh Takeuchi, Andras Boeszoermenyi, Paul W. Coote, Abhinav Dubey, Sven Hyberts, Gerhard Wagner, Haribabu Arthanari
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e5ddb6cd608240a3921746ce12e443cd
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spelling	oai:doaj.org-article:e5ddb6cd608240a3921746ce12e443cd2021-12-02T15:33:47ZMixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment10.1038/s41467-017-02767-82041-1723https://doaj.org/article/e5ddb6cd608240a3921746ce12e443cd2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02767-8https://doaj.org/toc/2041-1723Structure determination of large proteins by solution state NMR is challenging due to spectral overlap. Here the authors present a labeling strategy using 2-13C and 3-13C pyruvate as carbon source for E. coli, which increases the effective resolution of triple-resonance HNCA experiments and helps to overcome this problem.Scott A. RobsonKoh TakeuchiAndras BoeszoermenyiPaul W. CooteAbhinav DubeySven HybertsGerhard WagnerHaribabu ArthanariNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Scott A. Robson Koh Takeuchi Andras Boeszoermenyi Paul W. Coote Abhinav Dubey Sven Hyberts Gerhard Wagner Haribabu Arthanari Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
description	Structure determination of large proteins by solution state NMR is challenging due to spectral overlap. Here the authors present a labeling strategy using 2-13C and 3-13C pyruvate as carbon source for E. coli, which increases the effective resolution of triple-resonance HNCA experiments and helps to overcome this problem.
format	article
author	Scott A. Robson Koh Takeuchi Andras Boeszoermenyi Paul W. Coote Abhinav Dubey Sven Hyberts Gerhard Wagner Haribabu Arthanari
author_facet	Scott A. Robson Koh Takeuchi Andras Boeszoermenyi Paul W. Coote Abhinav Dubey Sven Hyberts Gerhard Wagner Haribabu Arthanari
author_sort	Scott A. Robson
title	Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
title_short	Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
title_full	Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
title_fullStr	Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
title_full_unstemmed	Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
title_sort	mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/e5ddb6cd608240a3921746ce12e443cd
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Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment

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