Protein conformation is of paramount importance in understanding biomolecular interactions.
Molecular interactions that involve conformational changes in the interacting molecules are more versatile. In the induced-fit model, two molecules bind optimally with each other only after conformational changes at their interface. Conformational changes may also take place away from the binding interface. This is often the prerequisite for functional activity. For protein like haemoglobin that shows allosteric behaviour, the binding of small molecules at a region of the protein affects its binding affinity with other molecules at a distant region.