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. 2018 Aug 13;293(39):15136–15151. doi: 10.1074/jbc.RA118.003290

Table 3.

Equilibrium binding constants and thermodynamic data for WASP BR mutants

Mutation Kda -Fold increase ΔG ΔΔG
μm kcal/mol cal/mol
WT 0.5 ± 0.1 −12.4
K225A 2.8 ± 0.3 5.6 −11.4 1.0
K226A 5.4 ± 0.8 10.8 −11.0 1.4
R227A 4.3 ± 0.4 8.6 −11.1 1.2
K225A/K226A 7.4 ± 1.2 14.8 −10.8 1.6
K225A/R227A 7.5 ± 1.0 15 −10.8 1.6
K226A/R227A 5.7 ± 0.7 11.4 −11.0 1.4
K225A/K226A/R227A 8.8 ± 1.0 17.6 −10.7 1.7
K230A 9.7 ± 0.7 19.4 −10.7 1.7
K231A 12.4 ± 1.0 24.8 −10.5 1.9
K232A 12.2 ± 1.0 24.4 −10.5 1.8
K230A/K231A 12.9 ± 1.2 25.8 −10.5 1.9
K230A/K232A 18.4 ± 2.1 36.8 −10.3 2.1
K231A/K232A 21.7 ± 2.8 43.4 −10.2 2.2
K230A/K231A/K232A 36.0 ± 3.1 72 −9.9 2.5
K225A/K226A/R227A/K230A/K231A/K232A 98.6 ± 10.9 197 −9.3 3.1

a The standard error from curve fitting is shown.