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Abstract

G protein-coupled receptors (GPCRs) play an essential role in signal transduction by transmitting extracellular stimuli into intracellular responses through activation of G proteins. The binding interaction between GPCRs and the Gα subunit of G proteins is a fundamental step in this process, initiating a cascade of downstream events. Interestingly, there are >800 members of the GPCR superfamily yet only 5 main classes of Gα subunit are needed to maintain homeostasis. How then, can this small set of Gα proteins bind to and recognize such a diverse family of receptors? The main goals of my thesis are: 1) to investigate this conserved interaction, primarily through studies of the visual GPCR rhodopsin and the high-affinity Gα-CT peptide, 2) to apply the insights gained to design novel tools for examining conformational equilibrium at rhodopsin (and other GPCRs) using biophysical and biochemical approaches, 3) to leverage our understanding of this key interaction to develop new ways to purify and study these vital receptors.

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