Fig. 4: Stopped-flow measurements of AQP3 and mutants.
From: Narrowed pore conformations of aquaglyceroporins AQP3 and GlpF
a The measured protein/phospholipid weight ratio of AQP3, AQP3 Y212F, and AQP3 Y212T proteoliposomes. Averaged values ± SEM and individual data points are plotted (n = 4 independently reconstituted liposome samples from the same purified proteins). Data are statistically analysed using multiple comparison Tukey test. P values are indicated. b, c Stopped-flow measurements under NaCl hyperosmotic conditions for AQP3, AQP3 Y212F, and AQP3 Y212T proteoliposomes and empty liposomes. Averaged water permeability Pf values ± SEM and individual data points are plotted (n = 4 independently reconstituted liposome samples from the same purified proteins) (b). Data are statistically analysed using multiple comparison Tukey test. P values are indicated. *P < 0.05 and ***P < 0.001. Representative time courses of normalised intensity change and fitted curves are shown (c). d, e Stopped-flow measurements under glycerol gradient conditions for AQP3, AQP3 Y212F, and AQP3 Y212T proteoliposomes and empty liposomes. Averaged glycerol permeability Pgly values ± SEM and individual data points are plotted (n = 4 independently reconstituted liposome samples from the same purified proteins) (d). Data are statistically analysed using multiple comparison Tukey test. P values are indicated. *P < 0.05, **P < 0.01, and ***P < 0.001. Representative time courses of normalised intensity change and fitted curves are shown (e). Source data are provided as a Source Data file.
