Abstract
We utilize supported lipid/protein bilayers to probe the dimerization of transmembrane (TM) helices in a membrane environment. The bilayers are formed by incubating substrates with liposomes containing the proteins, and are characterized using fluorescence recovery after photobleaching and imaging Forster resonance energy transfer (FRET). We show that the FRET signal, as a measure of TM helix dimerization, is the same in suspended liposomes and in surface-supported bilayers. This work is the first step toward the development of a new tool for probing the association of TM helices in lipid bilayers.
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