Table 2. Geometric and electrostatic properties of seven actin-binding proteins with G-actin.
| N c | Ion pairsa | |||
| ABP | Native complex | Transient Complex | Attractive | Repulsive |
| Profilin | 58 | 16 | K69-D288; R74-Cterm; R88-E167; K90-D286, D288; K125-E361, E364; E82-K113, R372 | K125-K373; D86-Cterm; E129-E364 |
| Twinfilin ADF-H 2 | 44 | 13 | Nterm-Cterm; R269-E334; K276, K294-E167; E296-R147; D298-R147, K328; E311-K291 | E311-D292 |
| Gelsolin domain 1 | 36 | 9 | R96-R147 | |
| WASP residues 431–446 | 26 | 7 | R431, R439-E167; K446-D25 | R431-R116 |
| Ciboulot residues 10–32 | 29 | 11 | K19-E167; K31-D24 | |
| Tβ4 residues 0–19 | 34 | 13 | K3-E167; K14-E334; K18-D24; K19-D25 | |
| DBP | 72 | 17 | K207-E167; R218-D288 E138-R147; E143-K328 E297, D298-K113 | R203-R147 |
a
Defined as any pair of charged residues that have a Coulomb interaction energy with a magnitude >13.8 kcal/mol (at dielectric constant = 4) in the native complex. This magnitude corresponds to a pair of unit charges at a distance of 6 Å. Residues before and after the dash are from the ABPs and G-actin, respectively.