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. 2015 Feb 20;4:e06074. doi: 10.7554/eLife.06074

Table 3.

Thermodynamic parameters for Btk PH-TH module binding to IP6 and IP4

DOI: http://dx.doi.org/10.7554/eLife.06074.016

Protein Ligand N Ka (×106) Kd (nM) ΔH (Kcal/mol) ΔS (cal/mol/deg)
Wild-type PH-TH IP6 1.1 ± 0.1 4.2 ± 0.3 238 ± 32 −1.1 ± 0.2 26.7
Wild-type PHTH IP4 0.9 ± 0.1 39 ± 11 26 ± 6 4.4 ± 0.1 49.5
PH-TH R28C/D24N IP6 0.7 ± 0.2 0.21 ± 0.03 4760 ± 700 −1.7 ± 0.6 17.5

The integrated heat from representative isothermal titration calorimetry experiments was fit with a one-binding site model. See methods for the details of data analysis.