Table 1.
Summary of results.
WH2 Constructs |
ΔrGd(kJ/mol) | Kd(µM) | Elongation rate (sub/s) |
max rate at 3µM (a.u.) |
ΔrGdf (kJ/mol) |
Kdf(µM) | Inhibition of nucleation |
---|---|---|---|---|---|---|---|
Sa | −0.3 ± 0.3 | 1.14 | 1.5 ± 0.2 | 4.1 ± 0.5 | N/D | 28 | +++ |
Sb | 5.9 ± 0.3 | 0.09 | 6.5 ± 0.7 | 3.5 ± 0.4 | −8 ± 3 | N/D | ++ |
Sc | 3.9 ± 0.1 | 0.21 (0.01) | 6.6 ± 1.3 | 3.2 ± 0.4 | −1.6 ± 0.3 | 2.0 | − |
Sd | 1.2 ± 0.1 | 0.62 (0.03) | 6.3 ± 0.5 | 3.1 ± 0.1 | −6.2 ± 0.6 | 13 | +++ |
Cs3 | 5.4 ± 0.3 | 0.11 | N/D | 4.0 ± 0.3 | −0.9 ± 0.5 | 1.4 | ++ |
S3d | 0.6 ± 0.2 | 0.78 | N/D | 5.2 ± 0.7 | −15 ± 5 | 500 | + |
Sc[qe] | 4.6 ± 0.2 | 0.15 | N/D | 2.1 ± 0.2 | −1.6 ± 0.4 | 1.9 | +++ |
Na | 0.7 ± 0.1 | 0.75 | N/D | 3.0 ± 0.3 | ## | ## | ++ |
Na[fs] | * | * | N/D | 5.5 ± 0.4 | N/D | N/D | − |
The values in parentheses are the predicted Kd’s for a second actin monomer binding to Sc3d as described for Figure 3B.
Na[fs] affinity is too weak to determine with confidence. It is > 30 µM.
Regression for Na with Kdf free did not converge.
N/D = not determined.