Effect of pH and surfactant on the protein: A perspective from theory and experiments.

In the present study, we are aimed to explore the bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) the interaction that can readily show the consequence of the change in concentration of protein with surfactants' various concentration and the different pH's, 4.0, 4.7, 7.0 of the medium through the many spectroscopic techniques. The BSA and SDS denaturation fully influenced by the pH. The results interpreted in terms of electrostatic and hydrophobic contributions to the stability of different phases formed in the system. Critical Micelle Concentration (CMC) of surfactant is influenced the protein folding and unfolding. The molecular docking supports the experiment data. This study demonstrates that the above and below the CMC of surfactant can significantly alter the binding interaction with the protein.