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. Author manuscript; available in PMC: 2014 Dec 23.
Published in final edited form as: Biochemistry. 2013 Dec 13;52(51):9223–9236. doi: 10.1021/bi400987k

Table 2.

Thermodynamic parameters for the binding of WW1 domain of WWOX to wildtype (PY3_WT) and single alanine mutants of ErbB4_PY3 peptide

Peptide Sequence Kd/μM ΔH/kcal.mol−1 TΔS/kcal.mol−1 ΔG/kcal.mol−1
PY3_WT graphic file with name nihms547377t4.jpg 144 ± 16 −6.21 ± 0.54 −1.24 ± 0.10 −5.25 ± 0.06
PY3_A−3 graphic file with name nihms547377t5.jpg 113 ± 21 −3.67 ± 0.23 +1.73 ± 0.34 −5.40 ± 0.11
PY3_A−2 graphic file with name nihms547377t6.jpg 151 ± 15 −6.19 ± 0.60 −1.32 ± 1.16 −5.22 ± 0.07
PY3_A−1 graphic file with name nihms547377t7.jpg 161 ± 29 −3.33 ± 0.42 +1.86 ± 0.52 −5.19 ± 0.11
PY3_A0 graphic file with name nihms547377t8.jpg NBD NBD NBD NBD
PY3_A+1 graphic file with name nihms547377t9.jpg NBD NBD NBD NBD
PY3_A+2 graphic file with name nihms547377t10.jpg 287 ± 37 −3.63 ± 0.30 +1.21 ± 0.37 −4.84 ± 0.08
PY3_A+3 graphic file with name nihms547377t11.jpg NBD NBD NBD NBD
PY3_A+4 graphic file with name nihms547377t12.jpg 275 ± 64 −4.02 ± 0.24 +0.85 ± 0.38 −4.87 ± 0.14
PY3_A+5 graphic file with name nihms547377t13.jpg 157 ± 18 −11.40 ± 1.41 −6.20 ± 1.48 −5.20 ± 0.07
PY3_A+6 graphic file with name nihms547377t14.jpg 135 ± 30 −4.78 ± 0.26 +0.52 ± 0.39 −5.29 ± 0.13

All parameters were obtained from ITC measurements at pH 7.0 and 25°C. Note that the alanine substitutions within the ErbB4_PY3 peptide are colored red and underlined, whilst the consensus residues within the PPXY motif are colored blue for clarity. All binding stoichiometries were fixed to unity. Errors were calculated from at least three independent measurements. All errors are given to one standard deviation. NBD indicates no binding determined due to weak interactions (Kd > 1mM).