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Figure 1
Purification and thermal-shift assay of A2AAR constitutive active mutants. (a) SDS–PAGE of purified WT and mutant A2AAR fusion proteins. (b) Size-exclusion chromatography plots (SECs) suggest that the A2AAR fusion proteins are mostly monomeric and of similar homogeneity. (c) Thermal-shift profiles and (d) melting temperature (Tm) plots of A2AAR WT and mutants in the apo state or in complex with the agonist (CGS21680) or antagonist (ZM241385). In the thermal-shift assay, 500 mM NaCl was added in parallel to each experimental buffer for strict comparison since sodium is an allosteric effector for A2AAR.

Volume 9| Part 3| May 2022| Pages 333-341
ISSN: 2052-2525