The mechanism of binding of molecular probe fluorescein to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding Center on human serum albumin molecule for fluorescein is determined. The amino acid residues of albumin molecule, participating in bindin
Raman spectroscopy in investigations of mechanism of human serum albumin denaturation under action of sodium dodecyl sulfate
โ Scribed by I.M. Vlasova; D.V. Polyansky; A.M. Saletsky
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 78 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1612-2011
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โฆ Synopsis
The mechanism of denaturation of human serum albumin under action of an anionic detergent โ sodium dodecyl sulfate (SDS) is investigated by Raman spectroscopy method. The quantitative contents of ฮฑ-helical segments and random packing segments of polypeptide chain of albumin at different concentrations of SDS and at different pH values of solutions are determined. It is shown, that more intensive denaturation under action of SDS, consisting in disturbance of secondary and tertiary structure of albumin, takes place at pH values of solution, smaller the isoelectric point of protein.
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The mechanism of binding of molecular probe eosin to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding center on human serum albumin molecule for eosin is determined. The amino acid residues of albumin molecule, participating in binding of eosin a
The comparative analysis of binding of three molecular fluorescent probes (fluorescein, eosin, and erythrosin), belonging to one homologous family, to human serum albumin (HSA) is made by Raman spectroscopy method. The binding of all three probes to binding Center I of HSA is registered. The charact