Table 1.

Biochemical characterization of the different complexes. The dissociation constants (K _d) were measured at equilibrium (295°K) by Surface Plasmon Resonance. Average values and standard errors are indicated (n ≥ 3). The binding energies (ΔG) are calculated from the K _d values

	wtYAP		Ser94AlaYAP
TEAD4	K d (nM)	ΔG (kcal/mol)	K d (nM)	ΔG (kcal/mol)
wt	17 ± 1	−10.58 ± 0.04	1807 ± 35	−7.83 ± 0.04
Tyr429Phe	57 ± 3	−9.88 ± 0.03	136 ± 6	−9.36 ± 0.01
Glu263Ala	129 ± 3	−9.39 ± 0.01	2221 ± 37	−7.70 ± 0.01
Tyr429Phe‐Glu263Ala	219 ± 2	−9.08 ± 0.01	178 ± 11	−9.20 ± 0.01