Conformational study of papain in the presence of sodium dodecyl sulfate in aqueous medium.
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 alpha-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.
Ghosh
Soumen
S
Centre for Surface Science, Department of Chemistry, Jadavpur University, Calcutta 700032, West Bengal, India. gsoumen70@hotmail.com
D002942:Circular Dichroism; D010206:Papain / Q000737:chemistry / Q000648:ultrastructure*; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014867:Water
D014867:Water; D012967:Sodium Dodecyl Sulfate; D010206:Papain