Abstract
Overexpression of biologically functional GPCRs and homogeneous purified protein solutions are required to enable structural studies and protein-based biophysical assay development. Iterative and time-consuming optimization cycles of protein engineering, expression, and purification are often needed to achieve the desired protein quantity and quality. Here, we describe the reconstitution of GPCRs in virus-like particles (VLPs) and their use in biophysical assays to characterize protein yield, stability, and small molecule ligand binding. This approach prevents the need for time-consuming detergent solubilization and protein purification during recombinant GPCR protein optimization.
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