W Stoeckenius

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We have used flash spectroscopy and pH indicator dyes to measure the kinetics and stoichiometry of light-induced proton release and uptake by purple membrane in aqueous suspension, in cell envelope vesicles and in lipid vesicles. The preferential orientation of bacteriorhodopsin in opposite directions in the envelope and lipid vesicles allows us to show(More)
Optical diffraction and image reconstruction can be used to correlate the electron microscope image of the biological membrane with its electron density projection. Such correlation shows that a single purple membrane particle contains 9 to 12 protein molecules--63 to 84 transmembrane alpha helices--a complexity two to ten times greater than that previously(More)
We have investigated the orientation of isolated fragments of Halobacterium halobium purple membrane (PM) adsorbed to poly-L-lysine-treated glass (PL-glass), by quanitative electron microscopy. Three lines of evidence support the conclusion that the cytoplasmic side of the membrane is preferentially absorbed. First, monolayer freeze-fracture reveals(More)
Halobacterium halobium is attracted by green and red light and repelled by blue-green and shorter wavelength light. a photochromic, rhodopsin-like protein in the cell membrane, sensory rhodopsin sR587, has been identified as the receptor for the long-wavelength and near-UV stimuli. Discrepancies between the action spectrum for the repellent effect of blue(More)
Solubilization of purple membrane with Triton X-100 yields Triton micelles containing bacteriorhodopsin monomers. The absorption maximum of dark-adapted solubilized bacteriorhodopsin is blue-shifted to 549 nm. Light adaption increases the absorbance by 4% and shifts the absorption maximum to 553 nm, i.e., the extent of light adaptation is considerably less(More)
The structure of the isolated cell envelope of Halobacterium halobium is studied by X-ray diffraction, electron microscopy, and biochemical analysis. The envelope consists of the cell membrane and two layers of protein outside. The outer layer of protein shows a regular arrangement of the protein or glycoprotein particles and is therefore identified as the(More)
Photoselection measurements with moderate excitation intensity on bacteriorhodopsin (bR) immobilized in a polyacrylamide gel soaked in 3 M KCl in the pH range 8.0-9.5 resulted in an unusual time-dependent anisotropy. In the microsecond region, the anisotropy exhibits a constant level that is considerably less than 2/5 theoretically expected for the(More)
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