hello, i want to know during calculation of free energy of binding for a ligand-receptor complex, how and how much desolvation energies contribution is?
is this represent to hydrophobic energy?
Hello. I'm working on protein-ligand interactions studies. Perhaps the following explanation and the attached papers could be useful.
DG = DH - T*DS (1)
Negative ΔG values which indicate spontaneous nature of adsorption process (between ligand and receptor).
ΔG values were lower than -10 kJ/mol suggesting a physical mechanism in the adsorption process between ligand and receptor.
On the other hand, if the –T.ΔS term in eq. 1 is larger in magnitude than ΔH term the adsorption process would be entropically-driven, i.e., the solvent molecules surrounding both ligand and receptor arranged themselves in a less orderly way when the adsorption take place.
Positive ΔS and DH indicate a hydrophobic interaction.
Regards
How would I explain that the system is Enthalpy or Entropy driven by the desovation energy???.
what I know is, desolvation energy affects both Enthalpy (more solvent more hydration) and entropy of the system(more disordered arrangement of solvent leads greater entropy).
it leads to one more question that in what condition the receptor-ligand complex is stronger, either more solvated in ordered arrangement or irregular arrangement.
Hi! And what does it mean a ligand-protein complex's desolvation energy of 3, 0 and -3? What is the difference between them? Thank you
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