Circular dichroism (CD) spectroscopy is a powerful technique used to investigate the structural and conformational properties of molecules, particularly in the field of biochemistry and biophysics. It is commonly employed in the study of biomolecules such as proteins, nucleic acids (DNA, RNA), and carbohydrates.

One of the main applications of circular dichroism spectroscopy is the characterization of protein secondary structure. CD spectra provide information about the folding patterns and conformational changes of proteins, helping researchers understand their three-dimensional structure, stability, and interactions. It can be used to study protein folding, protein-protein interactions, ligand binding, and structural changes induced by environmental factors like pH, temperature, or denaturants.

Circular dichroism spectroscopy is also utilized in the analysis of nucleic acids. It can provide insights into DNA and RNA structures, including helicity, stability, and interactions with ligands or proteins. CD can help determine the presence of secondary structural motifs such as helices, strands, or loops, as well as identify structural changes caused by sequence variations, modifications, or binding events.

Additionally, circular dichroism spectroscopy finds applications in the study of chiral molecules, supramolecular assemblies, and pharmaceutical compounds. It can be used to analyze the chirality and optical activity of organic molecules, examine the folding of synthetic polymers, investigate host-guest interactions in supramolecular chemistry, and assess the stereochemical properties of drug molecules.

In summary, circular dichroism spectroscopy is a versatile technique used in various fields, but it is particularly valuable in the characterization of protein and nucleic acid structures, aiding in the understanding of their properties and functions.