ArticleNature protocols2021
Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Article in Nature protocols, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 56 citations in OpenAlex.
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- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy.JACS Au · 2023Article
- Solid-state NMR structure determination of a membrane protein inScience advances · 2023Article
- GdJournal of the American Chemical Society · 2023Article
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- Highly bioresistant, hydrophilic and rigidly linked trityl-nitroxide biradicals for cellular high-field dynamic nuclear polarization.Chemical science · 2022Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
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- Stability of the nitroxide biradical AMUPol in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy.Angewandte Chemie (International ed. in English) · 2022Article
- Biological solid-state NMR: Integrative across different scientific disciplines.Journal of structural biology: X · 2022Article
- In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021Article
- Research Progress of NMR in Natural Product Quantification.Molecules (Basel, Switzerland) · 2021Review
- In Vivo Assembly of Artificial Metalloenzymes and Application in Whole-Cell Biocatalysis*.Angewandte Chemie (International ed. in English) · 2021Article
- Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy.Magnetic resonance (Gottingen, Germany) · 2021Article
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
For a long time, solid-state nuclear magnetic resonance (ssNMR) has been employed to study complex biomolecular systems at the detailed chemical, structural, or dynamic level. Recent progress in high-resolution and high-sensitivity ssNMR, in combination with innovative sample preparation and labeling schemes, offers novel opportunities to study proteins in their native setting irrespective of the molecular tumbling rate. This protocol describes biochemical preparation schemes to obtain cellular samples of both soluble as well as insoluble or membrane-associated proteins in bacteria. To this end, the protocol is suitable for studying a protein of interest in both whole cells and in cell envelope or isolated membrane preparations. In the first stage of the procedure, an appropriate strain of Escherichia coli (DE3) is transformed with a plasmid of interest harboring the protein of interest under the control of an inducible T7 promoter. Next, the cells are adapted to grow in minimal (M9) medium. Before the growth enters stationary phase, protein expression is induced, and shortly thereafter, the native E. coli RNA polymerase is inhibited using rifampicin for targeted labeling of the protein of interest. The cells are harvested after expression and prepared for ssNMR rotor filling. In addition to conventional
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