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A large number of integral proteins in eukaryotes do not traverse the membrane but are anchored in one or other leaflet of the bilayer through covalent attachment to a hydrocarbon chain. Several proteins, having the prion protein the causative agent of mad cow disease are stably anchored at the cell surface by covalent linkage of their C-terminal amino acid to the headgroup of a phosphatidylinositol lipid by an ethanolamine-phosphate-trimannose-glucosamine bridge, so-called GPI (glycosyl phosphatidylinositol)-anchored proteins. This difficult structure is built up by sequential addition of the individual sugar residues and ethanolamine phosphate to phosphatidylinositol. The C-terminal hydrophobic signal peptide is deleted from the protein in the lumen of the RER and the preformed GPI anchor added to the new exposed C- terminal amino acid.
figure: Lipid-modified proteins. (a) A glycosyl phosphatidylinositol-anchored protein (G, glucosamine; M, mannose; EtP, ethanolamine phosphate); (b) A myristoylated protein; (c) A prenylated protein; (d) a palmitoylated protein. Some proteins are also customized on Cys residues with covalently attached palmitate (C16:0) (palmitoylated proteins). These have some with membrane-spanning polypeptides (fig. 2d), some prenylated proteins and some myristoylated proteins. Various of the proteins having in cell signaling, like as the G proteins and the Ras family of proteins are lipid modified.
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Economic importance of obelia
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Q. In sickle cell anemia, a hereditary disease, there is replacement of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the s
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