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. 2008 Aug;49(8):1752–1761. doi: 10.1194/jlr.M800106-JLR200

Fig. 8.

Fig. 8.

Effect of pH on thermal unfolding kinetics of apoC-I complexes with DPPC or DSPC. A: CD data of apoC-I:DPPC disks (20 μg/ml protein in 5 mM Na phosphate buffer) recorded at selected pH in T-jumps from 25–80°C. Relaxation time τ1=1/k1 for the 1st kinetic phase obtained from exponential fitting of the T-jump data is plotted as a function of pH for apoC-I:DPPC (B) and apoC-I:DSPC disks (C). Plots in B and C are consistent with normal titration with pK 7.2 ± 0.1 (dashed line).