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Abstract
This dissertation investigates mechanisms of G protein-coupled receptor (GPCR) activation using reductionist approaches, focusing on the cannabinoid receptor CB1. Novel techniques were developed to purify CB1 and study dynamic structural changes via fluorescence spectroscopy, including the effects of an allosteric ligand. Additional work examined the structure and role of the receptor’s long N-terminus and generated CB1-specific antibodies, one of which is conformationally sensitive and modulates receptor activity. These findings advance understanding of GPCR structure-function relationships and provide tools for probing allosteric modulation and biased signaling in cannabinoid pharmacology.