Figure 2 | Scientific Reports

Figure 2

From: K336I mutant actin alters the structure of neighbouring protomers in filaments and reduces affinity for actin-binding proteins

Figure 2

Co-sedimentation of K336I actin filaments and alpha-actinin ABD. Solid lines show data fit using the following equation: [alpha-actinin ABD]bound/[F-actin] = [alpha-actinin ABD]free/Kd + [alpha-actinin ABD]free. The dissociation constants (Kd) of alpha-actinin ABD from actin filaments were as follows: K336I homo-filaments (blue circles), 30.0 ± 2.7 µM; WT homo-filaments (red squares), 15.1 ± 2.0 µM; and K336I/WT co-filaments (black triangles), 25.2 ± 2.2 µM (mean ± SE, N = 4). There is a statistically significant difference between WT homo-filaments and K336I homo-filaments (t-test, p < 0.001) as well as between WT homo-filaments and K336I/WT co-filaments (t-test, p < 0.01).

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