Circular Dichroism Spectroscopy Service

The determination of the secondary and tertiary structure of biomolecules, especially proteins and nucleic acids, is essential for the investigation of biomolecules' functions in their native, biologically active conformation. Circular dichroism (CD) is a powerful tool for understanding the secondary and tertiary structure of proteins, nucleic acids, as well as protein-ligand complexes. It can also characterize the binding interactions of non-immobilized molecules in the solution.

As an efficient method for secondary structure determination, CD has been widely used for characterization of protein structures. Specifically, when the amides chromophores on protein polypeptide backbone are aligned in arrays, their optical transitions are shifted or split into multiple transitions, as a result of 'exciton' interactions. Therefore, different structural elements present specific CD spectra. The protein aromatic chromophores, which have bands in the near UV region, are often in asymmetric environments and can be used to examine whether mutations change the tertiary structure of proteins. In addition, when chromophore ligands bind to target proteins, they may develop strong extrinsic CD bands that could also be used to detect binding.

Creative Biostructure provides CD services with advantages including but not limited to:

• Extensive spectroscopy facilities
• Professional and reliable data analysis
• Customized services to meet customer's specific needs
• Competitive price

Creative Biostructure promises to work closely with our customers to provide excellent services. Please feel free to contact us for more information.

References

1. Banerjee B, Misra G, Ashraf MT. Circular dichroism. Data Processing Handbook for Complex Biological Data Sources. Academic Press. 2019, 21-30.
2. Siligardi G, Hussain R. Circular Dichroism, Applications. Encyclopedia of Spectroscopy and Spectrometry. 2017, 293-298.
3. Greenfield N J. Using circular dichroism spectra to estimate protein secondary structure. Nature Protocols. 2006, 1(6): 2876-2890.