Abstract
The G–protein coupled receptor (GPCR) belongs to one of the most renowned protein super families. Over the past couple of decades, researchers have studied the dynamic dimer–monomer interconversion of GPCRs, potentially mediating their physiological functions. However, the generality and mechanism of this interconversion remain elusive. We developed the new technique for observing membrane proteins at the reconstituted lipid bilayer membrane formed at the narrow space between a glass substrate and Polydimethylsiloxane (PDMS). Using this technique, we discovered that the dynamic dimer formation is primarily regulated by the GPCR itself, rather than by micro– and nano–structures within a live cell.
