Fig. 4: Measurement of Gαiq:enNTS1ΔM4 complex affinity. | Nature Communications

Fig. 4: Measurement of Gαiq:enNTS1ΔM4 complex affinity.

From: Stabilization of pre-existing neurotensin receptor conformational states by β-arrestin-1 and the biased allosteric modulator ML314

Fig. 4: Measurement of Gαiq:enNTS1ΔM4 complex affinity.

a Microscale thermophoresis (MST) measured the affinity of Gαiq for NT8-13:enNTS1ΔM4 as 1.12 ± 0.1 μM (±SEM) using a single-site quadratic binding model. Data was collected as n = 3 biologically independent experiments in technical triplicates. Source data are provided as a Source Data file. b 1H 1D spectra of three unassigned Gαiq resonances exhibiting enNTS1ΔM4-dependent chemical shift perturbations. Spectra were recorded at 600 MHz with receptor concentrations of 64 μM and variable Gαiq concentrations: 0 μM (0×), 96 μM (1.5×), and 192 μM (3×).

Back to article page