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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.
Q. How many chambers do the mammalian heart and the bird heart have? Concerning temperature maintenance what is the benefit of the double and complete circulation of these animals?
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