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

Table 2.

Equilibrium binding constants and thermodynamic data for WASP GBD mutants

Mutation Kda -Fold increase ΔG ΔΔG
nm kcal/mol cal/mol
WT 0.5 ± 0.1 −12.4
I233A 26.4 ± 2.4 52.8 −10.1 2.3
K235A 8.0 ± 0.6 16.0 −10.8 1.6
I238A NDb >2000c
P241A 38.3 ± 3.0 76.6 −9.9 2.5
S242A 6.4 ± 0.9 12.8 −10.9 1.5
F244A 64.9 ± 7.7 129.8 −9.6 2.8
H246A 42.3 ± 4.5 84.6 −9.8 2.6
H249A 43.1 ± 2.3 86.2 −9.8 2.6
V250A 10.1 ± 1.1 20.2 −10.7 1.7
G251A 5.2 ± 0.5 10.4 −11.0 1.4
W252A 9.6 ± 0.9 19.2 −10.7 1.7
L267A 3.2 ± 0.5 6.4 −11.3 1.1
L270A 1.7 ± 0.4 3.4 −11.7 0.7
F271A 5.0 ± 0.8 10.0 −11.1 1.3
201–254 31.8 ± 2.7 63.6 −10.0 2.4

a The standard error from curve fitting is shown.

b ND (no binding) denotes data that could not be fitted to the binding isotherm.

c We assume a Kd of >1 μm (the limit of accurate direct SPA calculations).