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

Scott A. Robson; Koh Takeuchi; Andras Boeszoermenyi; Paul W. Coote; Abhinav Dubey; Sven Hyberts; Gerhard Wagner; Haribabu Arthanari

doi:10.1038/s41467-017-02767-8

Nature Communications (Jan 2018)

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

Scott A. Robson,
Koh Takeuchi,
Andras Boeszoermenyi,
Paul W. Coote,
Abhinav Dubey,
Sven Hyberts,
Gerhard Wagner,
Haribabu Arthanari

Affiliations

Scott A. Robson: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Koh Takeuchi: Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology
Andras Boeszoermenyi: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Paul W. Coote: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Abhinav Dubey: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Sven Hyberts: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Gerhard Wagner: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School
Haribabu Arthanari: Department of Biochemistry and Molecular Pharmacology, Harvard Medical School

DOI: https://doi.org/10.1038/s41467-017-02767-8
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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