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Binding free energy is defined as the free energy difference between the bound and completely unbound states. Although the bound state is a well-defined complex state, but the completely unbound state can be any states in which interactions between a protein and ligand of interest are negligible.
The binding free energy can be calculated using the rate constants kon and koff as G=Gbound-Gunbound=-kTln KeqC0=-kTln C0konkoff, where Keq is the binding equilibrium constant, C0 is the reference concentration of 1 mol/L, k is Boltzmanns constant and T is the temperature in Kelvin.
The change in Gibbs Free Energy, Go, is related to the dissociation constant for binding, KD, by the equation, Go = RT ln KD, where R is the gas constant [1.98722 cal/oKmol], and T is the absolute temperature.
Binding affinity refers to the strength of the interaction between a drug and its target protein. Gibbs free energy measures the stability and spontaneity of the drug-target complex, where the change in Gibbs free energy represents the associated energy change during the formation of the complex.
The binding affinity is the strength of the interaction between two (or more than two) molecules that bind reversibly (interact).
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The energy released due to the bond formation, or rather, interaction of the ligand and protein is termed in form of binding energy. The free energy of the favourable reaction is negative. Lesser the binding energy, better is the binding of the ligand and protein.
It is the energy required to create a system at constant pressure and temperature. Helmholtz free energy finds less application as the volume of the system should be constant. Gibbs free energy finds more application as the pressure of the system is constant.
To get an overview of Gibbs energy and its general uses in chemistry. Gibbs free energy, denoted G, combines enthalpy and entropy into a single value. The change in free energy, G, is equal to the sum of the enthalpy plus the product of the temperature and entropy of the system.

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