ArticleBiochemistry2013
Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles.Protein expression and purification · 2016Article
- Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- A new understanding of antibiotic action via solid-state NMR of cells with uniform isotopic labeling.Biophysical journal · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Recombinant proteins (RPs) are commonly expressed in bacteria followed by solubilization and chromatography. Purified RP yield can be diminished by losses at any step with very different changes in methods that can improve the yield. Time and labor can therefore be saved by first identifying the specific reason for the low yield. This study describes a new solid-state nuclear magnetic resonance approach to RP quantitation in whole cells or cell extracts without solubilization or purification. The method is straightforward and inexpensive and requires only ∼50 mL culture and a low-field spectrometer.
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Registered trials
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