Figure 4: Comparison of solution- and gas-phase unfolding experiments with two membrane proteins, ammonia channel (AmtB) and aquaporin Z (AqpZ), in the presence of different lipids.
From: Quantifying the stabilizing effects of protein–ligand interactions in the gas phase
(a) Thermal denaturation (Tm) measurements obtained by DSF of AmtB in the presence of PG, PS and PE at different lipid:protein ratios. Typical raw data are shown for the 10:1 lipid:protein ratio. The colour key applies to the whole figure. (b) Stabilization of AmtB by various lipids calculated using collision-induced unfolding (CIU)8. (c) Thermal denaturation of AmtB performed by CD in the presence of PG and PE, and (d) of AqpZ in the presence of PE and CDL. Typical raw data showing change in ellipticity at 220 nm are shown for both proteins with the different lipids. (e) Lipid stabilization of AqpZ measured using CIU8. Reported are average and s.e.m. from repeated measurements (n=3).
