The study of molecular interactions is an exponentially growing area in the field of structure-function relationships of biologically important molecules. On the molecular level, biological activity corresponds to the binding of a substrate, inhibitor, drug (low molecular weight) to a macromolecular receptor, usually a protein. 

CD is the ideal technique to determine the binding affinity and the ability to monitor a wide spectral region (140-700nm) enables the researcher to choose the appropriate region. The advantage of CD spectroscopy is that it measures the molecular binding affinity directly, without labelling or immobilising any of the ligand/receptor components and using small amounts of material.

 

The function and activity of a protein depends primarily on its 3D structure. The understanding of protein folding dynamics is a prerequisite for modelling confidently the native protein structure from the amino-acid sequence. The combination of simulated and observed electronic CD, vibrational CD and ROA spectra is going to be a powerful tool to address correctly the protein folding.

 

There is a growing interest in the structure-function relationship of nucleic acids, in particular for anti-cancer and anti-viral applications.