ArticleThe Journal of biological chemistry2008
Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
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139 citing papers in PubMed, 231 citations in OpenAlex.
- Negative design enables cell-free expression and folding of designed transmembrane β-barrels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Sited-Directed Fluorescence Spectroscopy for Studies on the Folding and Insertion of Proteins in Lipid Bilayers and Model Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analysis of the Kinetics of Folding and Insertion of β-Barrel Membrane Proteins by Gel-Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly.Communications biology · 2025Article
- A Practical Approach for Polarity and Quantity Controlled Assembly of Membrane Proteins into Nanoliposomes.Chembiochem : a European journal of chemical biology · 2025Article
- Overproduction of β-barrel outer membrane proteins inExtracellular vesicles and circulating nucleic acids · 2025Article
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Quantification of membrane fluidity in bacteria using TIR-FCS.Biophysical journal · 2024Article
- Sculpting conducting nanopore size and shape through de novo protein design.Science (New York, N.Y.) · 2024Article
- Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers.Microbiology spectrum · 2024Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Article
- Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023Article
- Protein-lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes.Nature chemistry · 2023Article
- TonB-Dependent Receptor Protein Displayed on Spores ofVaccines · 2023Article
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- Detergent headgroups control TolC folding in vitro.Biophysical journal · 2023Article
79 more citing papers are in PubMed but not listed here.
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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
Little is known about the dynamic process of membrane protein folding, and few models exist to explore it. In this study we doubled the number of Escherichia coli outer membrane proteins (OMPs) for which folding into lipid bilayers has been systematically investigated. We cloned, expressed, and folded nine OMPs: outer membrane protein X (OmpX), OmpW, OmpA, the crcA gene product (PagP), OmpT, outer membrane phospholipase A (OmpLa), the fadl gene product (FadL), the yaet gene product (Omp85), and OmpF. These proteins fold into the same bilayer in vivo and share a transmembrane beta-barrel motif but vary in sequence and barrel size. We quantified the ability of these OMPs to fold into a matrix of bilayer environments. Several trends emerged from these experiments: higher pH values, thinner bilayers, and increased bilayer curvature promote folding of all OMPs. Increasing the incubation temperature promoted folding of several OMPs but inhibited folding of others. We discovered that OMPs do not have the same ability to fold into any single bilayer environment. This suggests that although environmental factors influence folding, OMPs also have intrinsic qualities that profoundly modulate their folding. To rationalize the differences in folding efficiency, we performed kinetic and thermal denaturation experiments, the results of which demonstrated that OMPs employ different strategies to achieve the observed folding efficiency.
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