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. Author manuscript; available in PMC: 2010 Jan 20.
Published in final edited form as: Biochemistry. 2009 Jan 20;48(2):289–301. doi: 10.1021/bi8015668

Figure 3.

Figure 3

Panel a displays stopped-flow monitored changes in lipid fluorescence induced by addition of different HFP constructs to an aqueous solution containing membrane vesicles. Increased fluorescence is a result of mixing of lipids between different vesicles and this mixing is one consequence of vesicle fusion. The lines are color coded: HFPmn (black); HFPdm (red); HFPtr (blue); and HFPte (green). The total lipid concentration was 150 µM and the HFPmn, HFPdm, HFPtr, and HFPte concentrations were 1.50, 0.75, 0.50, and 0.37 µM, respectively, so that peptide strand:lipid = 0.01. The data were collected at 25 °C, the vesicle composition was 4:1 POPC:POPG, and the initial vesicle diameter was ~100 nm. Additional data (not shown) were obtained for HFPdm, HFPtr, and HFPte at 30, 35, and 40 °C. Each data set for each construct was analyzed as the sum of two exponential buildup functions. Panel b displays Arrhenius plots for the rate constants of the fast buildup function with legend: HFPdm (open square); HFPtr (open circle); and HFPte (open triangle). The best-fit lines are also displayed and result in the respective activation energies 41 ± 3, 26 ± 1, and 20 ± 1 kJ/mol.