Fig. 5: Fluorescence anisotropy of receptor-bound probes in active and G protein-uncoupled states.
From: Impact of secretin receptor homo-dimerization on natural ligand binding
Shown are the steady state anisotropy values of secretin fluorescent probes bound to WT SecR (left column) and non-dimerizing mutant SecR (right column) in the presence or absence of GppNHp, a non hydrolyzable analog of GTP. The values are shown as means ± S.E.M. from three independent experiments, and were analyzed using one-way ANOVA with Tukey post-test. Differences between active and G protein-uncoupled states (+GppNHp) are noted, *P < 0.05. Differences between the active states of WT SecR and mutant SecR are marked, #P < 0.05. Absolute values and statistical analysis are shown in Table 2.
