Abstract
G protein-coupled receptors (GPCRs) are integral membrane proteins involved in a wide range of cellular signaling processes. The structural and dynamic information is important in understanding the activation mechanism and essential for designing new drugs. However, despite the availability of high-resolution structures at different conformational states, the dynamics of those conformational states at the molecular level are still missing. Here, we used total internal reflection fluorescence (TIRF) imaging to investigate the conformational dynamics of the human A2A adenosine receptor (A2AAR), a representative class A GPCR, at the single-molecule level.
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