Table 1. Experimental and calculated rate constants for the association of seven actin-binding proteins with G-actin.
Experiment | Calculation | ||||||
ABP | PDB | k a (M−1 s−1) | I b (mM) | Ref. | k a (M−1 s−1) | k a0 (M−1 s−1) | ΔG el* (kcal/mol) |
Profilin | 2BTF | 1.4×107 | 110 | [5] | 1.04×107 | 3.60×105 | −1.99 |
Twinfilin ADF-H 2 | 3DAW | 2.36×107 | 110 | [7] | 1.22×107 | 7.90×105 | −1.62 |
Gelsolin domain 1 | 1EQY | 3.0×105 | 16 | [3] | 2.00×105 | 1.14×106 | 1.03 |
WASP WCA | 2A3Z | 4.3×107 | 65 | [6] | 1.65×107 | 2.53×106 | −1.11 |
Ciboulot domain 1 | 1SQK | 1.2×106 | 10 | [8] | 0.87×106 | 3.03×105 | −0.62 |
Tβ4 | 1SQK/1T44a | 1.7×106 | 5 | [9] | 4.04×106 | 7.52×105 | −0.99 |
DBP | 1KXP | 2.2×104 | 12 | [4] | 1.59×104 | 7.42×104 | 0.91 |
The complex of Tβ4 with G-actin was modeled by merging PDB entries 1SQK and 1T44 (see Methods for details).
Ionic strength.