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• W2169857885 abstract "Ghrelin receptor (GhrR) is a promising drug target because of its central role in energy homeostasis. GhrR, known for high constitutive activity, is thought to display multi-state conformations during activation and signaling. We used genetically encoded unnatural amino acids and bioorthogonal labeling reactions to engineer multiple fluorescent donor-acceptor pairs to probe ligand-directed structural changes in GhrR. We demonstrate how conformational dynamics of a G-protein-coupled receptor can be measured in reconstituted systems." @default.
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• W2169857885 date "2015-11-01" @default.
• W2169857885 modified "2023-10-16" @default.
• W2169857885 title "Bioorthogonal Labeling of Ghrelin Receptor to Facilitate Studies of Ligand-Dependent Conformational Dynamics" @default.
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• W2169857885 doi "https://doi.org/10.1016/j.chembiol.2015.09.014" @default.
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