Circular Dichroism Analysis of Protein Secondary Structure

The secondary structure of proteins refers to the local spatial structure of a peptide chain, which is a regular, asymmetric conformation maintained by hydrogen bonds resulting from the folding of the main chain. Examples include α-helix, β-sheet, β-turn, and random coil. These asymmetric structures give protein molecules circular dichroism. Circular Dichroism (CD) spectroscopy, also known as circular dichroic spectroscopy, analyzes the stereochemical structure based on the circular dichroism of the test substance and is a powerful tool for studying protein secondary structures.

The basic principle of circular dichroism spectroscopy in analyzing protein secondary structure is that proteins have different absorption coefficients for left and right circularly polarized light. When a protein solution is irradiated with plane-polarized light, there is a difference in absorption coefficients for left and right circularly polarized light. By plotting this difference in absorption coefficients (Δε) as the vertical axis and the wavelength of the plane-polarized light as the horizontal axis, the circular dichroism spectrum of the protein can be obtained. In this spectral curve, when the absorption coefficient of left circularly polarized light (εL) is greater than that of right circularly polarized light (εR), the difference Δε is positive, indicating that the protein is right-handed. Conversely, if εL is less than εR, a negative circular dichroism spectrum curve is obtained, indicating that the sample protein is left-handed.

Biotech company Baitech based oncircular dichroism analysisprovides a technology package for protein spatial conformation analysis services, including protein secondary and tertiary conformation analysis as well as protein interaction studies. Free consultation is welcome.

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