Figure 2 Relation between experimental free energy of solvation and binding enthalpy of the first hydration shell.
Following the discussion by Sakuma et al. (2014), such correspondence suggests that the relative binding enthalpy of the first hydration shell with six water molecules can describe the relative free energies of divalent cations in water.
The large binding enthalpy of the UP1 SL3ESS3 complex is consistent with enthalpies reported for other tandem RRM RNA interactions where the RNA strands are long enough to traverse both RRM domains.
The binding enthalpies of the specific and non-specific DNA binding to the protein differed significantly.
Solution calorimetry showed that TA bound to PC bilayers with a molar binding enthalpy of -8.3 kcal/mol and zeta potential measurements revealed that TA imparted a small negative charge to PC vesicles.
Unlike the case at pH 7.2, at pH 10, the displacement of glutamate by HW (approximately 80% deprotonated) was exothermic, with a favorable binding enthalpy of −5 ± 1 kcal/mol.
A 2 kcal/mol higher favorable binding enthalpy of SAHA compared to that of TSA could be attributed, at least in part, to the fact that the former ligand makes an additional hydrogen bond with the Asp 101 residue of the enzyme, which is evident from the structural data.
Subsequently, the interactions between dislocations and vacancies are dominated by electrostatics, with binding enthalpies of several eV in the vicinity of the dislocation core, superseding elastic effects.
This analysis yielded the thermodynamic parameters K (binding constant), enthalpy of binding (ΔH), entropy of binding (ΔS), and n, where n is the ratio of the metal ion to the substrate in the complex.
The intrinsic enthalpy (Δ H °ins) for protein ligand interaction, derived from the proton inventory data, provides the magnitude of binding enthalpy in the absence of the heat signal (due to protonation and/or deprotonation) contributed by the buffer medium.
