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- W1966854517 abstract "We study proteins at the surface of bilayer membranes using streptavidin and avidin bound to biotinylated lipids in a supported lipid bilayer (SLB) at the solid−liquid interface. Using X-ray reflectivity and simultaneous fluorescence microscopy, we characterize the structure and fluidity of protein layers with varied relative surface coverages of crystalline and noncrystalline protein. With continuous bleaching, we measure a 10−15% decrease in the fluidity of the SLB after the full protein layer is formed. We propose that this reduction in lipid mobility is due to a small fraction (0.04) of immobilized lipids bound to the protein layer that create obstacles to membrane diffusion. Our X-ray reflectivity data show a 40 Å thick layer of protein, and we resolve an 8 Å layer separating the protein layer from the bilayer. We suggest that the separation provided by this water layer allows the underlying lipid bilayer to retain its fluidity and stability." @default.
- W1966854517 created "2016-06-24" @default.
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- W1966854517 date "2007-05-01" @default.
- W1966854517 modified "2023-10-02" @default.
- W1966854517 title "Structure and Dynamics of Crystalline Protein Layers Bound to Supported Lipid Bilayers" @default.
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- W1966854517 doi "https://doi.org/10.1021/la063690e" @default.
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