Figure 4: Example fluorescence spectra of bimane-labelled arrestin mutants in the presence of enriched ROS-P membranes.
From: C-edge loops of arrestin function as a membrane anchor
The fluorescence (λex: 400 nm) of each bimane-labelled arrestin mutant (1 μM) was measured in the unbound state (grey spectra) or when bound to ROS-P (4 μM) control membranes (black spectra). The fluorescence in the presence of fatty-acid enriched ROS-P membranes is also shown: red, methyl palmitate; blue, N-tempoyl-palmitamide; orange, stearic acid; green, 5-doxyl-stearic acid. Note that fluorophores attached to sites on the membrane anchor (197, 339, 342, 344) display a spectral blue-shift upon complex formation with ROS-P (both dark-state and light-activated), indicating localization in a hydrophobic environment. Fluorescence spectra are normalized such that the fluorescence intensity of each mutant in the unbound state equals 1.
