Table 2.

Interaction Between the Different TEAD4 Proteins and the Synthetic Peptides hYAP^51–99 and hTAZ^14–56

Peptides	T m (°C)	ΔT m (°C)	K d (nM)
Non‐Acyl‐TEAD4
hYAP51–99	51.1 ± 0.2	7.4 ± 0.3	58 ± 3
hTAZ14–56	51.8 ± 0.1	8.1 ± 0.3	16 ± 1
Acyl‐TEAD4
hYAP51–99	59.1 ± 0.2	5.0 ± 0.3	21 ± 1
hTAZ14–56	59.3 ± 0.2	5.2 ± 0.3	5.3 ± 0.3
Cys367Ser
hYAP51–99	54.5 ± 0.0	5.8 ± 0.2	58 ± 4
hTAZ14–56	55.5 ± 0.0	6.8 ± 0.2	14 ± 1
Ref‐Cys367Ser
hYAP51–99	52.7 ± 0.2	7.2 ± 0.2	78 ± 5
hTAZ14–56	53.5 ±0.0	8.1 ± 0.2	18 ± 1

The melting temperature (T _m) of the TEAD4 proteins (1–2 µM) in the presence of the peptides (20 µM) was measured in a FTDA. The effect of the peptides on the thermal stability of the proteins was calculated as follows: ΔT _m =  $T_{\mathrm{m}}^{\text{peptide}+\text{protein}}$ – $T_{\mathrm{m}}^{\text{protein}\text{alone}}$. $T_{\mathrm{m}}^{\text{protein}\text{alone}}$ values are given in Table 1. Average and SEs of n ≥ 3 independent experiments are indicated. SE_{Δ T m =} ( ${\text{SE}}_{\text{Tmpeptide}+\text{protein}}^2$ +  ${\text{SE}}_{\text{Tmprotein}\text{alone}}^2$)^1/2. The dissociation constant (K _d) was measured at equilibrium by SPR at 10°C with the different proteins immobilized on sensor chips. Average and SE of n ≥ 3 independent experiments are indicated.