ArticleBiochimica et biophysica acta2012
Förster resonance energy transfer as a probe of membrane protein folding.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- 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
- Unveiling the Light Induced Energy Transfer Events in Water Soluble Benzothiazole Appended Borondipyrromethene: Synthesis, Photophysical Study, and Applications to Amyloid Binding.Chemistry, an Asian journal · 2026Article
- Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.Biochimica et biophysica acta. Biomembranes · 2020Article
- Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs.Biophysical journal · 2020Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- VAMP721 Conformations Unmask an Extended Motif for K+ Channel Binding and Gating Control.Plant physiology · 2017Article
- A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis.Biochemical Society transactions · 2016Review
- Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity.Journal of molecular biology · 2012Article
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Authors and funding
6 authors.
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Abstract
The folding reaction of a β-barrel membrane protein, outer membrane protein A (OmpA), is probed with Förster resonance energy transfer (FRET) experiments. Four mutants of OmpA were generated in which the donor fluorophore, tryptophan, and acceptor molecule, a naphthalene derivative, are placed in various locations on the protein to report the evolution of distances across the bilayer and across the protein pore during a folding event. Analysis of the FRET efficiencies reveals three timescales for tertiary structure changes associated with insertion and folding into a synthetic bilayer. A narrow pore forms during the initial stage of insertion, followed by bilayer traversal. Finally, a long-time component is attributed to equilibration and relaxation, and may involve global changes such as pore expansion and strand extension. These results augment the existing models that describe concerted insertion and folding events, and highlight the ability of FRET to provide insight into the complex mechanisms of membrane protein folding. This article is part of a Special Issue entitled: Membrane protein structure and function.
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