Structural Studies of Protein-Surfactant Complexes
- Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400 085 (India)
The structure of protein-surfactant complexes of two proteins bovine serum albumin (BSA) and lysozyme in presence of anionic surfactant sodium dodecyl sulfate (SDS) has been studied using small-angle neutron scattering (SANS). It is observed that these two proteins form different complex structures with the surfactant. While BSA protein undergoes unfolding on addition of surfactant, lysozyme does not show any unfolding even up to very high surfactant concentrations. The unfolding of BSA protein is caused by micelle-like aggregation of surfactant molecules in the complex. On the other hand, for lysozyme protein there is only binding of individual surfactant molecules to protein. Lysozyme in presence of higher surfactant concentrations has protein-surfactant complex structure coexisting with pure surfactant micelles.
- OSTI ID:
- 21136837
- Journal Information:
- AIP Conference Proceedings, Vol. 989, Issue 1; Conference: International conference on neutron and X-ray scattering 2007, Serpong and Bandung (Indonesia), 23-31 Jul 2007; Other Information: DOI: 10.1063/1.2906038; (c) 2008 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA); ISSN 0094-243X
- Country of Publication:
- United States
- Language:
- English
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