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- W2271129044 abstract "The ATP-synthase is a multi-subunit enzymic complex able to form ATP using the energy derived from a transmembrane proton gradient. Its activity is strictly lipid dependent. Relevant information on lipid–protein interaction and on polypeptide folding in the lipid bilayer has been obtained with the use of photoreactive phospholipids. These radioactive probes contain a photoactivatable group attached at a selected position of one fatty acid chain. On illumination a highly reactive intermediate is formed, which is able to react with neighbor molecules forming a covalent adduct. In the probe used in the experiment, the photoreactive nitroarylazido group is localized at the polar head group level and hence, it is believed to label only those polypeptide regions intercalated in the superficial part of the lipid bilayer. This chapter illustrates the pattern of labeling of the E. coli ATP-synthase obtained after incorporation of the enzyme in liposomes of egg lecithin tagged with 0.8% of the azidolecithin probe and illumination for 10' with a long wave U.V. lamp at 0°C. Most of the label is associated with polypeptide b, minor amounts with subunit c and β, while no radioactivity is associated with the other F1 subunits. Radioactivity was associated only with a large fragment containing the hydrophobic N-terminus. This peptide was attached to a solid support, sequenced and the radioactivity released at each step determined." @default.
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- W2271129044 date "1983-01-01" @default.
- W2271129044 modified "2023-09-23" @default.
- W2271129044 title "A HYDROPHOBIC PHOTOLABELLING STUDY OF THE ATP-SYNTHASE FROM ESCHERICHIA COLI" @default.
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- W2271129044 doi "https://doi.org/10.1016/b978-0-444-80540-9.50015-7" @default.
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