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- W4249565026 abstract "The molecular mechanisms of the folding reaction of an integral membrane protein, outer membrane protein A (OmpA), are investigated with Förster resonance energy transfer (FRET). Here, we report six mutants of the transmembrane portion of OmpA with intrinsic donor (tryptophan) and extrinsic acceptor (IAEDANS) in various locations of the protein to probe the evolution of distances during insertion and folding into lipid bilayers. Control experiments of donor-only and acceptor-only OmpA mutants have also been performed to determine the Förster distances (Ro) in the folded and unfolded states; the Ro values in both protein conformations are 21 Å. The FRET efficiencies evolve on three different timescales during the 240-minute observation window during folding, and are interpreted in terms of pore formation, bilayer traversal, and equilibration in the membrane. 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." @default.
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- W4249565026 date "2012-01-01" @default.
- W4249565026 modified "2023-10-16" @default.
- W4249565026 title "Förster Resonance Energy Transfer as a Probe of Membrane Protein Folding" @default.
- W4249565026 doi "https://doi.org/10.1016/j.bpj.2011.11.2198" @default.
- W4249565026 hasPublicationYear "2012" @default.
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