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. 2018 Mar 19;46(7):3791–3801. doi: 10.1093/nar/gky194

Table 1. Thermodynamic analysis of Leish4E-IP1 binding to LeishIF4E-1 as determined by isothermal titration calorimetry.

Titrants Leish4E-IP11–100 Leish4E-IP11–52
K (cal/mol) 1.148 × 107 ± 6.645 × 106 1.03 × 108 ± 4.54 × 107
ΔH (cal/mole) –3108 ± 80.36 –1.55 × 104 ± 281.8
ΔS (cal/mol/°) –21.9 –15.3
ΔG (kcal/mole) –2.56 –15.2
K D (nM) 87 9.7

Enthalpy changes (ΔH), entropy changes (ΔS), free energy changes (ΔG) and dissociation constants (KD) derived from ITC measurements at 25°C.