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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Main Authors:	Scott A. Robson, Koh Takeuchi, Andras Boeszoermenyi, Paul W. Coote, Abhinav Dubey, Sven Hyberts, Gerhard Wagner, Haribabu Arthanari
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-01-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-02767-8

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spelling	doaj-e5ddb6cd608240a3921746ce12e443cd2021-05-11T10:31:45ZengNature Publishing GroupNature Communications2041-17232018-01-019111110.1038/s41467-017-02767-8Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experimentScott A. Robson0Koh Takeuchi1Andras Boeszoermenyi2Paul W. Coote3Abhinav Dubey4Sven Hyberts5Gerhard Wagner6Haribabu Arthanari7Department of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolMolecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and TechnologyDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical SchoolStructure 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.https://doi.org/10.1038/s41467-017-02767-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Scott A. Robson Koh Takeuchi Andras Boeszoermenyi Paul W. Coote Abhinav Dubey Sven Hyberts Gerhard Wagner Haribabu Arthanari
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-01-01
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.
url	https://doi.org/10.1038/s41467-017-02767-8
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Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment

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