ArticleThe journal of physical chemistry. B2006
Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.
Article in The journal of physical chemistry. B, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs.Biophysical journal · 2020Article
- Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A.Biophysical journal · 2017Article
- Pyrene-Apelin Conjugation Modulates Fluorophore- and Peptide-Micelle Interactions.The journal of physical chemistry. B · 2017Article
- Complete Draft Genome Sequence of Escherichia coli JF733.Genome announcements · 2016Article
- Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.Biochimica et biophysica acta · 2015Article
- Insights into the structure and assembly of Escherichia coli outer membrane protein A.The FEBS journal · 2012Review
- Biophysics of α-synuclein membrane interactions.Biochimica et biophysica acta · 2012Review
- Förster resonance energy transfer as a probe of membrane protein folding.Biochimica et biophysica acta · 2012Article
- Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy.Biophysical journal · 2011Article
- Resolving the native conformation of Escherichia coli OmpA.The FEBS journal · 2010Article
- Oligo-(R)-3-hydroxybutyrate modification of sorting signal enables pore formation by Escherichia coli OmpA.Biochimica et biophysica acta · 2010Article
- Tryptophan probes at the alpha-synuclein and membrane interface.The journal of physical chemistry. B · 2010Article
- Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.Biochemistry · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Steady-state and time-resolved fluorescence measurements on each of five native tryptophan residues in full-length and truncated variants of E. coli outer-membrane protein A (OmpA) have been made in folded and denatured states. Tryptophan singlet excited-state lifetimes are multiexponential and vary among the residues. In addition, substantial increases in excited-state lifetimes accompany OmpA folding, with longer lifetimes in micelles than in phospholipid bilayers. This finding suggests that the Trp environments of OmpA folded in micelles and phospholipid bilayers are different. Measurements of Trp fluorescence decay kinetics with full-length OmpA folded in brominated lipid vesicles reveal that W102 is the most distant fluorophore from the hydrocarbon core, while W7 is the closest. Steady-state and time-resolved polarized fluorescence measurements indicate reduced Trp mobility when OmpA is folded in a micelle, and even lower mobility when the protein is folded in a bilayer. The fluorescence properties of truncated OmpA, in which the soluble periplasmic domain is removed, only modestly differ from those of the full-length form, suggesting similar folded structures for the two forms under these conditions.
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Registered trials
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