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Updated: Jul 19, 2025

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
DichroIDP: a method for analyses of intrinsically disordered proteins using circular dichroism spectroscopy
Andrew J Miles1, Elliot D Drew2,3, B A Wallace4
1Institute of Structural and Molecular Biology, Birkbeck University of London, London, WC1E 7HX, UK.
Abstract:
Intrinsically disordered proteins (IDPs) are comprised of significant numbers of residues that form neither helix, sheet, nor any other canonical type of secondary structure. They play important roles in a broad range of biological processes, such as molecular recognition and signalling, largely due to their chameleon-like ability to change structure from unordered when free in solution to ordered when bound to partner molecules. Circular dichroism (CD) spectroscopy is a widely-used method for characterising protein secondary structures, but analyses of IDPs using CD spectroscopy have suffered because the methods and reference datasets used for the empirical determination of secondary structures do not contain adequate representations of unordered structures. This work describes the creation, validation and testing of a standalone Windows-based application, DichroIDP, and a new reference dataset, IDP175, which is suitable for analyses of proteins containing significant amounts of disordered structure. DichroIDP enables secondary structure determinations of IDPs and proteins containing intrinsically disordered regions.
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