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. 2009 Dec 30;285(13):9981–9994. doi: 10.1074/jbc.M109.074005

TABLE 2.

Comparison of the stability and binding affinity of PDZ2240, PDZ2270, and PDZ2CT

PDZ2 variant Kd binding to C-CFTR70 ΔΔGbinding Kd binding to NHERF1-CT ΔΔGbinding M (urea denaturation) Cma ΔGb ΔΔGn-u0
μm kcal mol1 μm kcal mol1 kcal mol1m1 m kcal mol1 kcal mol1
PDZ2240 4.800 ± 0.300 0 803 ± 64 0 0.42 ± 0.20 1.9 ± 0.2 1.0 ± 0.1
PDZ2270 0.267 ± 0.011 −1.71 93.4 ± 5.9 −1.28 0.83 ± 0.05 3.9 ± 0.1 3.4 ± 0.1 2.4
PDZ2CT 5.300 ± 0.200 0.06 1230 ± 186 0.25 0.91 ± 0.13 4.2 ± 0.1 4.3 ± 0.2 3.3
PDZ2CT·FERM 0.202 ± 0.003 −1.88
PDZ2270(R153Q) 0.930 ± 0.045

a Cm is the urea concentration at which the protein is 50% unfolded.

b The free energies have been extrapolated to 0 m urea.