ArticleProtein science : a publication of the Protein Society2012
Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Cell-Free Protein Synthesis of Particulate Methane Monooxygenase into Nanodiscs.ACS synthetic biology · 2022Article
- Review
- Engineered Protein Model of the ATP synthase HScientific reports · 2018Article
- Reconstitution of Mitochondrial Membrane Proteins into Nanodiscs by Cell-Free Expression.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Cell-free methods to produce structurally intact mammalian membrane proteins.Scientific reports · 2016Article
- Yeast knockout library allows for efficient testing of genomic mutations for cell-free protein synthesis.Synthetic and systems biotechnology · 2016Article
- Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination.Cellular and molecular life sciences : CMLS · 2014Article
- Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.Journal of bacteriology · 2013Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
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4 authors.
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Abstract
NMR structure determination of large membrane proteins is hampered by broad spectral lines, overlap, and ambiguity of signal assignment. Chemical shift and NOE assignment can be facilitated by amino acid selective isotope labeling in cell-free protein synthesis system. However, many biological detergents are incompatible with the cell-free synthesis, and membrane proteins often have to be synthesized in an insoluble form. We report cell-free synthesis of subunits a and c of the proton channel of Escherichia coli ATP synthase in a soluble form in a mixture of phosphatidylcholine derivatives. In comparison, subunit a was purified from the cell-free system and from the bacterial cell membranes. NMR spectra of both preparations were similar, indicating that our procedure for cell-free synthesis produces protein structurally similar to that prepared from the cell membranes.
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