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• W2104792316 abstract "elsewhere (Jones and Chapman, 1995a, b), but more to discuss the rationale of such approaches, including considArtificial membrane systems are being used increas- erations and controls. It is hoped that the references ingly to study the function and role of plant membrane provided will supply the reader with any more detailed proteins, particularly solute transporters which cata- information that is required. lyse counter-exchange of metabolites. Performing Model bilayer systems are often used for studying such studies requires (i) solubilization of the protein membrane transport as they negate many of the probwith a suitable surfactant, (ii) functional reconstitution lems associated with the use of membrane vesicles of the protein in a well characterized liposome system. ( Klingenberg, 1985; Hochstadt et al., 1975) and some Much of the technology has been derived from studies types of intact plant organelles ( Tetlow et al., 1996). The on non-plant systems and there are many pitfalls of model system approach involves removal of membrane which to be wary before applying it to a new protein. proteins, or specific protein(s), from the cell or purified This short review outlines the key parameters which organelle, followed by functional reconstitution into a should be considered when attempting the study of closed bilayer system produced specifically for that purplant membrane proteins in artificial lipid bilayers, pose. Transport measurements can then be made. The including types of surfactants, lipid composition advantage of such a system is that conditions on either of vesicles, membrane permeability, and protein side of the membrane can be manipulated in order to orientation. characterize the function of a single transporter or transport complex in isolation from other cellular or membrane" @default.
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• W2104792316 date "1999-12-01" @default.
• W2104792316 modified "2023-09-23" @default.
• W2104792316 title "Proteoliposomes and plant transport proteins" @default.
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• W2104792316 doi "https://doi.org/10.1093/jxb/50.341.1715" @default.
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