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. Author manuscript; available in PMC: 2011 Nov 2.

Published in final edited form as: Biochemistry. 2010 Nov 2;49(43):9181–9189. doi: 10.1021/bi101155r

Thermal unfolding of hA₂aR-His₁₀ monitored via CD at 222 nm (A) or via fluorescence intensity (463 nm) of a thiol-reactive fluorescent probe, CPM (B), for unliganded receptors (closed circles), receptors with 100 μM CHA agonist (open triangles), with 1000 μM theophylline antagonist (crosses), and reduced with 1 mM TCEP (open circles). Lines represent fit to a single-transition folding model for experimental data (points). Error bars represent standard deviation from the average of 3 or more trials. Note that CPM and TCEP are not compatible, as background fluorescence in the presence of TCEP was too large for detection of changes with temperature.

Thermal unfolding of hA₂aR-His₁₀ monitored via CD at 222 nm (A) or via fluorescence intensity (463 nm) of a thiol-reactive fluorescent probe, CPM (B), for unliganded receptors (closed circles), receptors with 100 μM CHA agonist (open triangles), with 1000 μM theophylline antagonist (crosses), and reduced with 1 mM TCEP (open circles). Lines represent fit to a single-transition folding model for experimental data (points). Error bars represent standard deviation from the average of 3 or more trials. Note that CPM and TCEP are not compatible, as background fluorescence in the presence of TCEP was too large for detection of changes with temperature.