If anyone knows about these terminologies please let me know!
Binding energy, Ligand efficiency, Inhibition constant (µM), Inter molecular energy, Vander Waals desolvation energy, Electrostatic energy, Total energy, Torsional energy and Unbound energy.
Binding energy is a measure of the affinity of ligand-protein complex, or is the difference between the energy of complex and the sum of energies of each molecule separately.
Ligand efficiency is binding energy per atom of ligand to protein.
Intermolecular energy is the energy between non-bounded atoms, that is the energy between atoms separated by 3-4 bonds or between atoms in different molecules.
Desolvation energy is the electrostatic and/or van der Waals energy lose of the interaction between ligand or protein and solvent upon binding.
Electrostatic energy is the non-bounded energy, which is different from electrostatic desolvation energy. It is the change on the electrostatic non bounded energy of ligand or protein upon binding.
Total energy is the sum of changes of all energetic terms included in scoring function of lingand or protein upon binding, plus the changes upon binding of the entropic terms.
Torsion energy is related to dihedral term of internal energy.
Inhibition constant is an indication of how potent an inhibitor is, it is concentration required to produce half maximum inhibition.
Binding energy is a measure of the affinity of ligand-protein complex, or is the difference between the energy of complex and the sum of energies of each molecule separately.
Ligand efficiency is binding energy per atom of ligand to protein.
Intermolecular energy is the energy between non-bounded atoms, that is the energy between atoms separated by 3-4 bonds or between atoms in different molecules.
Desolvation energy is the electrostatic and/or van der Waals energy lose of the interaction between ligand or protein and solvent upon binding.
Electrostatic energy is the non-bounded energy, which is different from electrostatic desolvation energy. It is the change on the electrostatic non bounded energy of ligand or protein upon binding.
Total energy is the sum of changes of all energetic terms included in scoring function of lingand or protein upon binding, plus the changes upon binding of the entropic terms.
Torsion energy is related to dihedral term of internal energy.
Inhibition constant is an indication of how potent an inhibitor is, it is concentration required to produce half maximum inhibition.
I have two question beside to my question. Is there any relationship between these energies and secondly what is the selection creteria of the top docking pose.
Hi..for selection criteria, you can consider the docking free energy score, its inhibition constant and also the Hydrogen bonds.
Top docking pose, consider the binding energy (lowest), Inhibition constant (lowest) and more number of H-bond interactions with active site of the protein.
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