ArticleChembiochem : a European journal of chemical biology2022
Rapid Estimation of Membrane Protein Orientation in Liposomes.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026Review
- Fluorescence-Based Ion Transport Assays Using Proteoliposomes.Bio-protocol · 2026Article
- Structural mechanism of lipid modulation of pentameric ligand-gated ion channel activity.bioRxiv : the preprint server for biology · 2025Article
- The Conformational Equilibria of a Human GPCR Compared between Lipid Vesicles and Aqueous Solutions by IntegrativeJournal of the American Chemical Society · 2025Article
- Dissecting Structural Requirements of Leucinostatin A Derivatives for Antiprotozoal Activity and Mammalian Toxicity.Journal of medicinal chemistry · 2025Article
- Modulating Liposome Surface Charge for Maximized ATP Regeneration in Synthetic Nanovesicles.ACS synthetic biology · 2024Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- A Fluorescence-based Approach Utilizing Self-labeling Enzyme Tags to Determine Protein Orientation in Large Unilamellar Vesicles.Bio-protocol · 2022Article
- Article
- Experimental platform for the functional investigation of membrane proteins in giant unilamellar vesicles.Soft matter · 2022Article
- Rapid Estimation of Membrane Protein Orientation in Liposomes.Chembiochem : a European journal of chemical biology · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The topological organization of proteins embedded in biological membranes is crucial for the tight interplay between these enzymes and their accessibility to substrates in order to fulfil enzymatic activity. The orientation of a membrane protein reconstituted in artificial membranes depends on many parameters and is hardly predictable. Here, we present a convenient approach to assess this important property independent of the enzymatic activity of the reconstituted protein. Based on cysteine-specific chemical modification of a target membrane protein with a cyanine fluorophore and a corresponding membrane-impermeable fluorescence quencher, the novel strategy allows rapid evaluation of the distribution of the two orientations after reconstitution. The assay has been tested for the respiratory complexes bo
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