ArticleProtein science : a publication of the Protein Society2013
High-yield membrane protein expression from E. coli using an engineered outer membrane protein F fusion.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- A nondestructive membrane engineering method using an amphiphilic polymer.Protein science : a publication of the Protein Society · 2024Article
- Functional and structural characterization of Hyp730, a highly conserved and dormancy-specific hypothetical membrane protein.MicrobiologyOpen · 2021Article
- Membrane Protein Production and Purification from Escherichia coli and Sf9 Insect Cells.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Construction of a bacterial surface display system based on outer membrane protein F.Microbial cell factories · 2019Article
- On the Spatial Organization of mRNA, Plasmids, and Ribosomes in a Bacterial Host Overexpressing Membrane Proteins.PLoS genetics · 2016Article
- Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016Review
- Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.Nature protocols · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Obtaining high yields of membrane proteins necessary to perform detailed structural study is difficult due to poor solubility and variability in yields from heterologous expression systems. To address this issue, an Escherichia coli-based membrane protein overexpression system utilizing an engineered bacterial outer membrane protein F (pOmpF) fusion has been developed. Full-length human receptor activity-modifying protein 1 (RAMP1) was expressed using pOmpF, solubilized in FC15 and purified to homogeneity. Using circular dichroism and fluorescence spectroscopy, purified full-length RAMP1 is composed of approximately 90% α-helix, and retains its solubility and structure in FC15 over a wide range of temperatures (20-60°C). Thus, our approach provides a useful, complementary approach to achieve high-yield, full-length membrane protein overexpression for biophysical studies.
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