Interaction of trypsin with sodium dodecyl sulfate in aqueous medium: a conformational view

The conformational behavior of a globular protein, trypsin has been studied in presence of an anionic surfactant, sodium dodecyl sulfate (SDS) in aqueous medium by different techniques, such as, viscometry, circular dichroism, fluorimetry, Fourier transform infra-red, UV-vis absorption, dynamic light scattering and nuclear magnetic resonance. The results indicate that the viscosity of the mixture increases above the critical micelle concentration of SDS micelle supporting an expansion of a protein coil in the cluster. The spectroscopic techniques show the change of the conformation, i.e., the change of the values of alpha-helicity, beta-sheet, and random-coil of trypsin in the presence of SDS, and ultimately unfolding of trypsin occurs due to strong electrostatic repulsion of micellar clusters of the protein-surfactant complexes.