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Updated: Mar 6, 2026

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
Circular Dichroism and Fluorescence Spectroscopy to Study Protein Structure and Protein-Protein Interactions in
Mareike Kessenbrock1, Georg Groth2
1Institute of Biochemical Plant Physiology, Heinrich-Heine University Düsseldorf, Universitätsstraße 1, D-40225, Düsseldorf, Germany.
Abstract:
Circular dichroism (CD) spectroscopy is an invaluable technique to analyze secondary structure and functional folding of recombinant purified proteins. CD spectroscopy can also be applied to detect changes in protein secondary structure related to the pH or redox conditions found in different cellular compartments or to the interaction with other molecules. Another biophysical technique to monitor conformational changes and interaction with small molecule ligands or biological macromolecules is protein fluorescence spectroscopy making use of the aromatic amino acid tryptophan as a sensitive intrinsic fluorescent probe. Here, we describe the application of CD and tryptophan fluorescence spectroscopy to study soluble and membrane proteins of the ethylene signaling pathway.
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