[1] The conformational changes usually take place during intermolecular association, such as protein–protein interaction or protein–ligand binding.
A binding partner changes the conformation of a biomolecule (e.g. a protein) to enable or disable its biochemical activity.
Methods for analysis of conformation activity relationship vary from in silico[2] or using experimental methods such as X-ray crystallography and NMR where the conformation before and after activity can be compared statically or using dynamic methods such as multi-parametric surface plasmon resonance, dual-polarisation interferometry or circular dichroism where the kinetics as well as degree of conformational change can be quantified.
Static experimental techniques include X-ray crystallography and NMR.
Dynamic experimental techniques include multi-parametric surface plasmon resonance, dual-polarization interferometry, and circular dichroism.