Fig. 3
From: Defining a conformational ensemble that directs activation of PPARγ
Helix 12 solvent exposure is distinct for the active and inactive helix 12 conformations. a 19F NMR spectra of delipidated apo PPARγC313A,K502C-BTFA bound to 0.2 molar equivalent of GW1929 (left), and T0070907-bound PPARγK502C-BTFA with excess free BTFA, at the indicated concentrations of D2O. Due to the high binding affinity of GW1929 (4 nM), all three expected peaks (two apoprotein peaks and one GW1929 peak) are present in slow exchange on the NMR time scale, allowing analysis of the three conformations simultaneously. b D2O solvent isotope-induced changes, plotted as % D2O vs. change 19F NMR chemical shift values for various peaks; a dotted gray line is shown to highlight no D2O-induced change in 19F NMR chemical shift. These experiments were performed once
