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Spectroscopic Probe Analysis of Protein-Surfactant Interactions : The BSNSDS System
| Content Provider | Semantic Scholar |
|---|---|
| Author | Xue-Gong Aronson, Moshe |
| Copyright Year | 2001 |
| Abstract | The interactions and structure of complexes formed between bovine serum albumin (BSA) and the anionic surfactant sodium dodecyl sulfate has been investigated by spectroscopic probe techniques. Steady state and time-resolved fluorescence, electron spin resonance, and deuterium NMR spectroscopy have been employed as a multitechnique approach to investigate the structures which occur along the proteinsurfactant isotherm. Three models of the protein-surfactant complex are considered. The results of the multitechnique approach are consistent with a structure which is predominantly of the "necklace and bead" type in which the unfolded protein wraps around surfactant micelles. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://turroserver.chem.columbia.edu/PDF_db/publications_551_600/578.pdf |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Bos taurus Contour line Deuterium Electron Spin Resonance Spectroscopy Fluorescence Interaction Serum Albumin Serum Albumin, Bovine Serum Metabolome Database Sodium Dodecyl Sulfate Spectroscopy, Near-Infrared Steady state |
| Content Type | Text |
| Resource Type | Article |
