Since the discovery of circular dichroism by Jean-Baptiste Biot, Augustin Fresnel, and Aimé Cotton in the last century, the phenomenon has been widely used in various fields. Circular dichroism (CD) is the difference in absorption of left-handed circularly polarized light (L-CPL) and right-handed circularly polarized light (R-CPL), occurs when a molecule contains one or more chiral chromophores (light absorbing groups).
Different structural elements present specific CD spectra, so the use of this technology to measure the CD produced by specific molecules within a certain wavelength range can be applied to many fields. Its applications include: studying chiral molecules of various types and sizes; exploring the secondary structure/conformation of macromolecules; obtaining kinetic and thermodynamic information, such as how the secondary structure changes with environmental conditions or the interactions with other molecules.
Figure 1. Schematic representation of the Circular Dichroism instrument configuration (Pignataro, M.F.; et al.)
Creative Proteomics is professional experts in the application of circular dichroism. We have introduced many advanced spectroscopy equipment, including circular dichroism spectroscopy, variable temperature circular dichroism, magnetic circular dichroism, and high-sensitivity polarimetry, etc. The technology platform is managed by experienced experts and is regularly upgraded to enhance performance.
Creative Proteomics' circular dichroism (CD) service can be used to analyze all aspects of the structure and conformation of different samples, providing information on the structure of proteins, nucleic acids, peptides and other organic molecules in the sample. The analysis we can provide includes, but is not limited to:
Protein Structure Analysis: CD can be used to study the secondary structure elements of proteins, such as alpha helices, beta sheets, and random coils. It can provide information about protein folding, stability, and conformational changes.
Nucleic Acid Conformation: CD can analyze the secondary structure and conformational changes of nucleic acids, such as DNA and RNA. It can provide insights into their helical structure, base stacking, and interactions with ligands or proteins.
Learn more about RNA circular dichroism assay.
Peptide Conformation and Folding: CD analysis can investigate the secondary structure elements and folding patterns of peptides. It can determine the presence of alpha helices, beta strands, turns, and random coil conformations.
Ligand Binding Studies: CD can be used to examine the interaction between biomolecules and small molecules, such as drugs or ligands. It can provide information about changes in the secondary structure upon ligand binding and determine the binding affinity.
Protein Folding and Stability: CD analysis can assess the folding kinetics and thermodynamic stability of proteins. It can monitor changes in the protein structure under different conditions, such as temperature, pH, or presence of denaturants.
Conformational Changes: CD can detect conformational changes in biomolecules induced by external factors, such as temperature, pH, or ligand binding. It can provide insights into structural transitions and conformational dynamics.
It is worth mentioning that we have developed algorithms with higher reliability, as well as objective methods for comparing spectra, which can be used for unbiased comparative studies of biopharmaceuticals and biosimilars.
Customers can choose different technology platforms according to project requirements, or contact us directly for consultation, and our expert team will provide you with customized experimental procedures.
Creative Proteomics is an international biotechnology company dedicated to research in molecular interactions and other related fields. The circular dichroism platform we constructed has the characteristics of high sensitivity and efficiency, and the data obtained can be directly used for article publication. Our one-stop service aims to save customers time and money.