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Following protein-glycosaminoglycan polysaccharide interactions with differential scanning fluorimetry.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2012; Vol. 836, pp. 171-82. - Publication Year :
- 2012
-
Abstract
- 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.
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 836
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 22252635
- Full Text :
- https://doi.org/10.1007/978-1-61779-498-8_12