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- W957202469 abstract "Publisher Summary This chapter discusses the properties and spatial arrangement of components in preinitiation complexes of eukaryotic protein synthesis. The topography of proteins in eukaryotic ribosomes has been studied so far mainly by cross-linking and immune electron microscopy. The composition of 42 protein complexes cross-linked by DBI within the 40-S ribosomal subunit from the rat liver has been analyzed. By this procedure, 25 out of the 30 proteins contained within the small ribosomal subunit were identified as the components of cross-linked protein dimers. For proteins S4, S20, and S3, eight, seven, and six neighbors were found, respectively; three to five neighbors were identified for 16 other proteins and the remaining six proteins could only be cross-linked to one or two other proteins. Topological mapping of proteins on ribosomal particles is possible also by using antibodies against ribosomal proteins in combination with electron microscopy (immune electron microscopy). This method was first applied for the localization of E. coli ribosomal proteins. The principle of this technique involves the reaction of ribosomal particles with antibodies against individual ribosomal proteins and subsequent electron microscopic investigation of the ribosome–antibody complexes after negative staining." @default.
- W957202469 created "2016-06-24" @default.
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- W957202469 date "1985-01-01" @default.
- W957202469 modified "2023-10-14" @default.
- W957202469 title "Properties and Spatial Arrangement of Components in Preinitiation Complexes of Eukaryotic Protein Synthesis" @default.
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- W957202469 doi "https://doi.org/10.1016/s0079-6603(08)60351-7" @default.
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