Figure 1
The changes in free energy (ΔG) that drive molecular recognition. The equilibrium is biased towards ligand binding when the thermodynamically favourable interactions (for example electrostatic attraction, hydrogen bonding, burial of hydrophobic groups and van der Waals forces) are larger than the thermodynamically unfavourable contributions (for example ligand desolvation, reduction in entropy associated with complexation and structural distortion of the ligand or protein, for example during induced-fit interactions). |