Abstract
To test the hypothesis that differences in lipid bilayer and membrane protein hydrophobic thicknesses can brings about a mechanism of lipid molecular sorting by proteins, computer simulations and Fluorescence Resonance Energy Transfer experiments (between NBD-labeled lipids as donor and retinal as acceptor) were carried out on Bacteriorhodopsin reconstituted in DLPC/DSPC mixtures. This study took advantage of the non-ideal mixing behavior of DLPC and DSPC and the fact that the average lipid acyl-chain length depends on temperature. At low temperature, in the gel-gel coexistence region, BR is found associated with the short-chain lipid DLPC. At moderate temperature, in the fluid-gel coexistence region, BR still shows preference for DLPC but now stands at the fluid-gel boundary. At high temperature, in the fluid-fluid phase, the theoretical data shows preference of BR for the longchain DSPC at the expense of the short-chain DLPC molecules.
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Dumas, F., Lebrun, MC., Sperotto, M.M., Mouritsen, O.G., Tocanne, JF. (1998). Consequences of Hydrophobic Matching on the Lateral Distribution of Lipids Around Bacteriorhodopsin Reconstituted in DLPC/DSPC Mixtures. In: Op den Kamp, J.A.F. (eds) Lipid and Protein Traffic. NATO ASI Series, vol 106. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-51463-0_29
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DOI: https://doi.org/10.1007/978-3-642-51463-0_29
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