Small-angle neutron scattering study of structural evolution of different phases in protein solution

Small-angle neutron scattering (SANS) has been used to study the structural evolution of different phases in protein solution leading to crystallization, denaturation elation. The protein solution under crystallization mostly consists of monomers and dimers, and higher-mers are not observed lis they are perhaps formed in very small numbers. The, on-set and the rate of crystallization strongly depend on the salt concentration. Protein denaturation oil 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 it fractal structure. Rheology of these gels shows it strong dependence on varying pH or protein concentration, whereas the structure of such gels is found to he similar.