ArticleJournal of the American Chemical Society2014
Selective methyl labeling of eukaryotic membrane proteins using cell-free expression.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Human cells for human proteins: Isotope labeling in mammalian cells in suspension for functional NMR studies.Protein science : a publication of the Protein Society · 2026Article
- Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine.RSC chemical biology · 2026Article
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein.Protein science : a publication of the Protein Society · 2024Article
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- Protein deuterationChemical communications (Cambridge, England) · 2024Article
- E. coli "Stablelabel" S30 lysate for optimized cell-free NMR sample preparation.Journal of biomolecular NMR · 2023Article
- Improved spectral resolution of [Journal of biomolecular NMR · 2023Article
- Stabilization of pre-existing neurotensin receptor conformational states by β-arrestin-1 and the biased allosteric modulator ML314.Nature communications · 2023Article
- Cell-free synthesis of proteins with selectivelyMagnetic resonance (Gottingen, Germany) · 2023Article
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Local Deuteration Enables NMR Observation of Methyl Groups in Proteins from Eukaryotic and Cell-Free Expression Systems.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- Improving yields of deuterated, methyl labeled protein by growing in HJournal of biomolecular NMR · 2018Article
- Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data.Journal of biomolecular NMR · 2017Article
- The membrane anchor of the transcriptional activator SREBP is characterized by intrinsic conformational flexibility.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- Affordable uniform isotope labeling with (2)H, (13)C and (15)N in insect cells.Journal of biomolecular NMR · 2015Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Structural characterization of membrane proteins and other large proteins with NMR relies increasingly on perdeuteration combined with incorporation of specifically protonated amino acid moieties, such as methyl groups of isoleucines, valines, or leucines. The resulting proton dilution reduces dipolar broadening producing sharper resonance lines, ameliorates spectral crowding, and enables measuring of crucial distances between and to methyl groups. While incorporation of specific methyl labeling is now well established for bacterial expression using suitable precursors, corresponding methods are still lacking for cell-free expression, which is often the only choice for producing labeled eukaryotic membrane proteins in mg quantities. Here we show that we can express methyl-labeled human integral membrane proteins cost-effectively by cell-free expression based of crude hydrolyzed ILV-labeled OmpX inclusion bodies. These are obtained in Escherichia coli with very high quantity and represent an optimal intermediate to channel ILV precursors into the eukaryotic proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.