Fig. 4.
Actin-binding properties of WT and mutant dystrophins. F-actin-binding isotherms for 0.5 μM WT (A), K18N (B), and L54R (C) dystrophins measured by high-speed cosedimentation with increasing amounts of F-actin. Symbols represent three independent experiments plotted on the same graph and curves represent the best fit of the aggregate cosedimentation data. (D) The Kd’s obtained from fitted data for WT and each mutant protein were significantly different for K18N and L54R (p < 0.05). The Bmax values obtained from the same dataset were significantly different (p < 0.05) for L54R, D165V A168D, and L172H.