The superfamily of G protein coupled receptors mediate cellular responses to a variety of sensory stimuli, hormones, growth factors, and neurotransmitters and are targets of a number of widely prescribed drugs. Signal transduction by these receptors occurs when an activated receptor interacts with a trimeric G protein in the cytoplasm, causing the G protein to release a bound molecule of GDP and to replace it with a molecule of GTP.
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Despite their importance, approaches for analyzing the structures of transmembrane proteins are still slow and difficult compared to the standard technologies available for soluble proteins. Only about twenty structures of eukaryotic transmembrane proteins have been determined to date, compared with tens of thousands of structures of soluble proteins.
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Most biochemical experiments are performed using huge numbers of molecules in bulk solution. In many cases, this leads to significant averaging over populations of molecules that may differ from each other. We are developing a technology for using fluorescence measurements on single molecules of membrane proteins to learn about the heterogeneity of conformations that such molecules adopt in the process of carrying out their molecular functions.
Learn more about Single Molecule Fluorescence Analysis of Conformational Changes in Transmembrane Transporters