Studies of the structural changes invoked in proteins by the binding of the glycosaminoglycan (GAG) polysaccharide portion of proteoglycans are of increasing importance to research in a wide range of fields, from biochemistry and molecular biology to biotechnology and medicine. One important aspect is the degree of stabilisation or destabilisation induced in a protein by the binding of these anionic materials, and this can affect enzyme activity, the stability of complexes, folding and the formation of aggregates, including those in neurodegenerative processes. A simple method, able to determine the effect of interactions with GAG polysaccharides on protein stability is described, based on the propensity of a fluorescent dye-Sypro™ Orange-to present differentiable fluorescence emission spectra following contact with exposed core amino acid residues. The method requires only commonly available and inexpensive equipment and is suitable for a multi-well format, allowing multiple readings to be made simultaneously. © 2012 Springer Science+Business Media, LLC.
CITATION STYLE
Uniewicz, K. A., Ori, A., Rudd, T. R., Guerrini, M., Wilkinson, M. C., Fernig, D. G., & Yates, E. A. (2012). Following protein-glycosaminoglycan polysaccharide interactions with differential scanning fluorimetry. Methods in Molecular Biology, 836, 171–182. https://doi.org/10.1007/978-1-61779-498-8_12
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