How to Analyze the Spectrum in Protein Circular Dichroism (CD) Analysis
When analyzing the circular dichroism (CD) spectra of proteins, the following aspects are commonly considered:
1. Peak Shape Identification
Begin by examining the shape of the peaks in the CD spectra. Proteins with α-helix structures typically exhibit characteristic negative peaks near 208 nm and 222 nm. In contrast, β-sheet structures generally produce one positive and one negative peak, often observed around 218 nm.
2. Peak Intensity Comparison
Comparing the intensities of these peaks allows for an estimation of the relative proportions of different secondary structures. For instance, more intense negative peaks are often indicative of a higher α-helix content.
3. Quantitative Analysis
Dedicated software tools—such as DichroWeb, SELCON, and CONTIN—can be employed to analyze the spectral data and estimate the relative amounts of α-helix, β-sheet, β-turns, and random coil structures. These programs work by comparing the experimental spectra against reference datasets derived from proteins with well-characterized secondary structures.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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