Abstract
Small‐angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) during its unfolding in presence of protein denaturating agents urea and surfactant. On addition of urea, the BSA protein unfolds for urea concentrations greater than 4 M and acquires a random coil configuration with its radius of gyration increasing with urea concentration. The addition of surfactant unfolds the protein by the formation of micelle‐like aggregates of surfactants along the unfolded polypeptide chains of the protein. The fractal dimension of such a protein‐surfactant complex decreases and the overall size of the complex increases on increasing the surfactant concentration. The conformation of the unfolded protein in the complex has been determined directly using contrast variation SANS measurements by contrast matching the surfactant to the medium. Results of DLS measurements are found to be in good agreement with those obtained using SANS.
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