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• W958008972 abstract "Immunoelectron microscopy (IEM) is one of several techniques that have proved useful for the elucidation of the structural organization of the ribosome, and has provided considerable information on the topography of the proteins on the ribosomal surface. The principle of IEM is to bind a purified IgG antibody, specific to a single ribosomal protein, to the appropriate ribosomal subunit; the bivalent antibody dimerizes two subunits which can then be examined under the electron microscope. The location of the bound antibody on the antigenic determinant of a particular protein can thus be made visible. Application of the different IEM methods described above for the localization of the ribosomal proteins on the surface of the ribosomal subunits from E. coli has led to the current model of the arrangement of the ribosomal proteins. So far, 16 proteins from the small subunit and 17 proteins from the large subunit have been localized. There is also an excellent agreement between the IEM results and the topographical data obtained by neutron scattering for the 30S subunit. If all the topographical data are taken together, the location of the remaining five proteins of the 30S subunit still to be mapped by IEM can be deduced." @default.
• W958008972 created "2016-06-24" @default.
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• W958008972 date "1988-01-01" @default.
• W958008972 modified "2023-09-25" @default.
• W958008972 title "[35] Localization of ribosomal proteins on the surface of ribosomal subunits from Escherichia coli using immunoelectron microscopy" @default.
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• W958008972 doi "https://doi.org/10.1016/s0076-6879(88)64066-3" @default.
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