Table 4.

Thermodynamic parameters obtained from ITC measurements for the binding of WW2 domain of YAP2 to wildtype (WT) and single alanine mutants of the WBP2_PY3 peptide

Peptide	Sequence	Kd/μM	ΔH/kcal.mol−1	TΔS/kcal.mol−1	ΔG/kcal.mol−1
PY3_WT	SQPPPPPYYPPE	116 ±1	−13.51 ±0.23	−8.14 ±0.22	−5.37 ±0.01
PY3_Q-3A	SAPPPPPYYPPE	107 ±4	−8.92 ±0.01	−3.49 ±0.03	−5.42 ±0.02
PY3_P-2A	SQAPPPPYYPPE	111 ±3	−13.53 ±0.03	−8.13 ±0.01	−5.40 ±0.02
PY3_P-1A	SQPAPPPYYPPE	117 ±1	−8.97 ±0.08	−3.60 ±0.08	−5.37 ±0.01
PY3_P0A	SQPPAPPYYPPE	368 ±18	−9.60 ±0.20	−4.91 ±0.17	−4.69 ±0.03
PY3_P+1A	SQPPPAPYYPPE	590 ±44	−4.61 ±0.28	−0.19 ±0.23	−4.41 ±0.04
PY3_P+2A	SQPPPPAYYPPE	163 ±9	−8.02 ±0.06	−2.84 ±0.10	−5.17 ±0.03
PY3_Y+3A	SQPPPPPAYPPE	199 ±8	−3.46 ±0.27	+1.60 ±0.25	−5.06 ±0.02
PY3_Y+4A	SQPPPPPYAPPE	104 ±2	−9.85 ±0.18	−4.41 ±0.17	−5.44 ±0.01
PY3_P+5A	SQPPPPPYYAPE	79 ±4	−10.43 ±0.35	−4.82 ±0.38	−5.61 ±0.03
PY3_P+6A	SQPPPPPYYPAE	105 ± 2	−12.41 ±0.03	−6.97 ±0.04	−5.44 ±0.01

The alanine substitutions within the WBP2_PY3 peptide are underlined for clarity. Binding stoichiometries generally agreed to within ±10%. Errors were calculated from at least three independent measurements. All errors are given to one standard deviation.