Small-angle neutron scattering (SANS) has been used to study the structural evolution of different phases in protein solution leading to crystallization, denaturation and gelation. The protein solution under crystallization mostly consists of monomers and dimers, and higher-mers are not observed as they are perhaps formed in very small numbers. The onset and the rate of crystallization strongly depend on the salt concentration. Protein denaturation on addition of surfactant occurs due to the formation of micelle-like clusters along the unfolded polypeptide chains of the protein. The structure of such protein{surfactant complex is found to be independent of the size of the micelles in their pure surfactant solutions. The structure of temperature-induced protein gels shows a fractal structure. Rheology of these gels shows a strong dependence on varying pH or protein concentration, whereas the structure of such gels is found to be similar.

Small angle neutron scattering (SANS) has been used to study conformational changes in protein bovine serum albumin (BSA) as induced by varying temperature and in the presence of protein denaturating agents urea and surfactant. BSA has pro-late ellipsoidal shape and is found to be stable up to 60°C above which it denaturates and subsequently leads to aggregation. The protein solution exhibits a fractal structure at temperatures above 64°C, with fractal dimension increasing with temperature. BSA protein is found to unfold in the presence of urea at concentrations greater than 4 M and acquires a random coil Gaussian chain conformation. The conformation of the unfolded protein in the presence of surfactant has been determined directly using contrast variation SANS measurements by contrast matching surfactant molecules. The protein acquires a random coil Gaussian conformation on unfolding with its radius of gyration increasing with increase in surfactant concentration

We report dynamic light scattering and small angle neutron scattering studies of the pressure-induced structural transition of nonionic micelles of surfactant polyoxyethylene 10 lauryl ether (C12E10) in the pressure range 0 to 2000 bar. Measurements have been performed on 1 wt% C12E10 in aqueous solution with and without the addition of KF. Micelles undergo sphere to lamellar structural transitions as the pressure is increased. On addition of KF, rod-like micelles exist at ambient pressure, which results in rod-like to lamellar structural transition at a much lower pressure in the presence of KF. Micellar structural transitions have been observed to be reversible.