beta-casein is a protein which forms micelles in aqueous solvents. The
magnitude and the range of the weight-average interactions between th
e diverse solute particles are inferred from small-angle neutron scatt
ering measurements made on various beta-casein solutions. Well above t
he critical micelle concentration (CMC), these interactions are repuls
ive. They weaken with decreasing protein concentration, and finally be
come strongly attractive near the CMC. Although indispensable for mice
lle formation this fact has never been reported so far.