Circular Dichroism Analysis
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Circular dichroism (CD) spectroscopy is a relatively simple and effective technique that is commonly used to determine the secondary and tertiary structure of antibody molecules. Creative Proteomics has built an advanced circular dichroism platform for in-depth characterization of the advanced high order structure of antibody drugs. The instrument is equipped with temperature and titer modules to further investigate the effects of temperature, pH, ionic strength and other factors on protein folding state and stability. We are committed to providing you with the most comprehensive structural characterization information.
Principles of Circular Dichroism Spectroscopy
Circular dichroism works by using the circular dichroism of proteins and the different absorption of left and right circularly polarized light by asymmetric molecules to analyze the structure of proteins. The main photoactive groups in proteins or peptides are peptide bonds, aromatic amino acid residues and disulfide bonds. When the absorption of plane circularly polarized light is different, an absorption difference is created. The presence of this absorption difference results in a difference in the amplitude of the polarized light vector, and the circularly polarized light becomes elliptically polarized, i.e., the circular dichroism of the protein. The secondary and higher structures of protein and peptide samples can be analyzed to some extent by the circular dichroism scanner.
Application of Circular Dichroism in Antibody Drug Structural Characterization
Our advanced assay technology can help clients to obtain structural information of antibody drugs in the following areas.
- Determination of secondary structure
The scanning pattern of circular dichroism in the far-ultraviolet region can reflect the information about the arrangement of protein peptide bonds. What is obtained by calculation is the proportion of protein secondary structure, i.e., the proportion of α-helices, β-folds, corners, and irregular coils.
The scanning pattern of circular dichroism in the near-ultraviolet region can reflect the information about the arrangement of residues such as tryptophan, phenylalanine, tyrosine, and other residues of the protein side-chain chromophore groups and the changes in the microenvironment of disulfide bonds.
CD can detect conformational changes in the protein induced by changes in temperature, pH, and solvent conditions. It helps customers gain insight into the stability and folding of antibody drugs.
Through CD technology, we provide our customers with quantitative information on the secondary structure content and the degree of conformational changes in antibody drug molecules.
Why Choose Us?
Creative Proteomics provides professional circular dichroism services for the analysis and determination of the spatial conformation of proteins. This technique has the following advantages over traditional methods:
- Fast, simple and accurate study of the conformation of proteins and peptides in solution.
- Small sample volumes are required and can be measured in dilute solutions.
- No molecular weight or size limitation.
- Highly sensitive to secondary and tertiary structural changes, capable of detecting small changes.
Service Ordering Process
Creative Proteomics provides you with advanced circular dichroism technology and analytical services for the comprehensive characterization of high-level structural information of antibody drugs. Contact us to learn more about circular dichroism spectroscopy. We will be happy to assist you.
