ArticleBioinformatics (Oxford, England)2013
Charge asymmetry in the proteins of the outer membrane.
Article in Bioinformatics (Oxford, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Recent advances in host models in studying virulence factors and pathogenesis ofFrontiers in cellular and infection microbiology · 2025Review
- Ultrasonication outperforms electroporation for extracellular vesicle cargo depletion.Extracellular vesicle · 2024Article
- Protein-lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes.Nature chemistry · 2023Article
- General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Asymmetric Lipid Vesicles: Techniques, Applications, and Future Perspectives as an Innovative Drug Delivery System.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Drug‑resistantExperimental and therapeutic medicine · 2023Review
- Membrane Barrels Are Taller, Fatter, Inside-Out Soluble Barrels.The journal of physical chemistry. B · 2021Article
- PutativeFrontiers in microbiology · 2021Article
- The Outer Membrane Proteins OmpA, CarO, and OprD ofFrontiers in microbiology · 2020Review
- A comprehensive computational study of amino acid interactions in membrane proteins.Scientific reports · 2019Article
- Peptoid drug discovery and optimization via surface X-ray scattering.Biopolymers · 2019Review
- Article
- Identification of a novel post-insertion step in the assembly of a bacterial outer membrane protein.Molecular microbiology · 2018Article
- Tight Turns of Outer Membrane Proteins: An Analysis of Sequence, Structure, and Hydrogen Bonding.Journal of molecular biology · 2018Article
- Efflux Pumps Represent Possible Evolutionary Convergence onto the β-Barrel Fold.Structure (London, England : 1993) · 2018Article
- Statistically derived asymmetric membrane potentials from α-helical and β-barrel membrane proteins.Scientific reports · 2018Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins.Molecular microbiology · 2017Article
- Outer membrane protein design.Current opinion in structural biology · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
motivationOuter membrane beta-barrels (OMBBs) are the proteins found in the outer membrane of bacteria, mitochondria and chloroplasts. There are thousands of beta-barrels reported in genomic databases with ∼2-3% of the genes in gram-negative bacteria encoding these proteins. These proteins have a wide variety of biological functions including active and passive transport, cell adhesion, catalysis and structural anchoring. Of the non-redundant OMBB structures in the Protein Data Bank, half have been solved during the past 5 years. This influx of information provides new opportunities for understanding the chemistry of these proteins. The distribution of charges in proteins in the outer membrane has implications for how the mechanism of outer membrane protein insertion is understood. Understanding the distribution of charges might also assist in organism selection for the heterologous expression of mitochondrial OMBBs.
resultsWe find a strong asymmetry in the charge distribution of these proteins. For the outward-facing residues of the beta-barrel within regions of similar amino acid density for both membrane leaflets, the external side of the outer membrane contains almost three times the number of charged residues as the internal side of the outer membrane. Moreover, the lipid bilayer of the outer membrane is asymmetric, and the overall preference for amino acid types to be in the external leaflet of the membrane correlates roughly with the hydrophobicity of the membrane lipids. This preference is demonstrably related to the difference in lipid composition of the external and internal leaflets of the membrane.
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