Study of chemically unfolded β-casein by means of small-angle neutron scattering

β-casein is a flexible amphiphilic milk protein which forms an unfolded conformation in presence of very high denaturant concentrations. The structure of β-casein formed at the bulk was studied by small-angle neutron scattering (SANS). The value of the second virial coefficient of the protein solutions indicates that the interactions between the polypeptide chain and solvent are repulsive. The protein conformation is similar to an excluded volume chain. The corresponding values of the contour length, L, the statistical length, b and the apparent radius of the chain cross-section, Rc are given.