Peptide Circular Dichroism Secondary Structure Measurement

Circular Dichroism (CD) spectroscopy is a technique for analyzing the molecular structure of optically active substances based on their circular dichroism. It holds an important position in the identification of secondary structures of proteins. Both peptides and proteins are optically active biomolecules with asymmetric spatial structures. Their circular dichroism can be used to analyze secondary structures such as α-helices, β-sheets, and β-turns through CD spectroscopy.

The spatial structure of substances like peptides is determined mainly by measuring the ellipticity [θ] of the molecules. The ellipticity [θ] indicates the degree to which optically asymmetric peptide molecules absorb left and right circularly polarized light differently. Peptides have two main UV absorption peaks: one at 280 nm caused primarily by aromatic side chains (mainly Tyr, Trp, Phe) and another at wavelengths below approximately 230 nm, caused by electronic transitions within the peptide backbone and other amino acid side chains. Analyzing the CD spectrum near the 230 nm region can thus reveal the conformation of the peptide backbone.

Biotech company offers high-efficiency and preciseprotein/peptide secondary structure CD analysisservice packages that can be used to determine whether the expressed and purified proteins/peptides are folded or mutated, whether these affect their conformation or stability, and can also be used to study protein/peptide interactions. Free consultations are welcome.

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