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- W2105113670 abstract "Membranes prepared from Torpedo californica electroplax containing acctylcholine receptors have been studied by X-ray diffraction and electron microscopy. X-ray diffraction data suggest that acetylcholine receptor molecules traverse the endplate membrane, extending 15 ± 5 Å on one side of the bilayer and some 55 ± 5 Å on the other, with an overall length normal to the membrane of 110 Å. Lattices of acetylcholine receptor have the symmetry of the crystallographic plane group p1, with one molecule per unit cell. A low-resolution projection of the surface structure of receptor arrays was determined by reconstruction of images from electron micrographs. The resolution of the image is ~ 20 Å in the plane of the membrane. The electron density profile through the membrane, derived from X-ray diffraction of vesicle dispersions and of oriented membranes, has been analyzed to resolutions of 20 and 13 Å, respectively. The high-angle X-ray scattering pattern was observed to a resolution of 1.7 Å. Maxima in the scattering pattern were analyzed in terms of the state of the lipids and secondary structure in the membranes. Sharp maxima in the scattering pattern indicate that long stretches of secondary structure are present in the receptor-containing membranes. The receptor membranes contain repeating structural units of length 80 Å (5.2 Å repeat) oriented perpendicular to the membrane plane, and uninterpreted components greater than 90 Å in length with a basic repeat of 6.3 Å." @default.
- W2105113670 created "2016-06-24" @default.
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- W2105113670 date "1977-11-01" @default.
- W2105113670 modified "2023-10-15" @default.
- W2105113670 title "Structural studies of a membrane-bound acetylcholine receptor from Torpedo californica" @default.
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- W2105113670 doi "https://doi.org/10.1016/0022-2836(77)90264-9" @default.
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