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- W75863854 abstract "Past studies in one of our laboratories (RRT) have emphasized reversible protein-protein crosslinking to map the overall protein topography of each ribosomal subunit and the 70S ribosome of Escherichia coli(Sommer and Traut, 1974; Traut et al., 1980; Lambert and Traut, 1981; Lambert et al., 1983). The approach has also been used to identify proteins at the binding sites for initiation factors (Boileau et al., 1983) and one of the elongation factors, EF-G. The other laboratory (DGG) has taken a different approach to the localization of both RNA and protein components of the ribosome, immune electron microscopy. The two approaches are often complementary and, together with the other experiments that directly implicate functional sites, they provide a more complete picture of ribosomal function domains. For example, a combination of affinity labeling with puromycin and immune electron microscopy located protein L23 at the 50 S peptidyl transferase center (Olson and Glitz, 1979; Grant et al., 1983; Olson et al., 1982). Identification of crosslinks between L23 and other proteins extends the understanding of the protein topography of this functional domain." @default.
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- W75863854 date "1986-01-01" @default.
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- W75863854 title "Protein Topography of Ribosomal Functional Domains: Effects of Monoclonal Antibodies to Different Epitopes in Escherichia coli Protein L7/L12 on Ribosome Function and Structure" @default.
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- W75863854 doi "https://doi.org/10.1007/978-1-4612-4884-2_17" @default.
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