| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9678404 | Colloids and Surfaces B: Biointerfaces | 2005 | 8 Pages |
Abstract
The interactions between a globular protein, papain and the anionic surfactant, sodium dodecyl sulfate (SDS) have been investigated in aqueous medium using fluorimetric, circular dichroism, Fourier transform infra-red, UV-vis spectrophotometric, dynamic light scattering, and nuclear magnetic resonance techniques. The conformational change of papain in aqueous solution has been studied in the presence of SDS. The results show the high α-helical content and unfolded structure of papain in the presence of SDS due to strong electrostatic repulsion leading to a “necklace and bead model” in protein-surfactant complexes.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Soumen Ghosh,