| Following protein-glycosaminoglycan polysaccharide interactions with differential scanning fluorimetry. | |
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MedLine Citation:
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PMID: 22252635 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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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. |
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Authors:
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Katarzyna A Uniewicz; Alessandro Ori; Timothy R Rudd; Marco Guerrini; Mark C Wilkinson; David G Fernig; Edwin A Yates |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Methods in molecular biology (Clifton, N.J.) Volume: 836 ISSN: 1940-6029 ISO Abbreviation: Methods Mol. Biol. Publication Date: 2012 |
Date Detail:
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Created Date: 2012-01-18 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9214969 Medline TA: Methods Mol Biol Country: United States |
Other Details:
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Languages: eng Pagination: 171-82 Citation Subset: IM |
Affiliation:
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Institute of Integrative Biology, University of Liverpool, Liverpool, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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