Abstract
H+ transporting ATP synthase is a remarkable molecular machine that catalyzes the synthesis of ATP by use of two coupled motors, F0 and F1. The use of the H+ electrochemical gradient drives rotation of the c ring, which couples with the F1 domain to induce conformational changes that catalyze the formation of ATP form ADP and inorganic phosphate. The FO section of ATP synthase is primarily embedded in the membrane, so it is possible that lipid contacts and composition could play a role in proton translocation and function. Cardiolipin, a phospholipid that comprises a significant portion of the inner mitochondrial membrane, has been observed using cryo-electron microscopy.8 These lipid effects could be essential for normal function. A protocol for reconstitution of E. coli ATP synthase has been developed, with emphasis on different techniques for detergent removal and liposome recollection.
How to Cite
O’Keefe, D., (2018) “Development of a Reconstitution Protocol for ATP Synthase with Various Lipids”, Capstone, The UNC Asheville Journal of Undergraduate Scholarship 31(1).
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