Many natural proteins self-assemble in complex ways, either to fulfill their biological function or introduce particular properties, such as high strength and toughness. We report the morphological transition in water from a spherical to rod-like shape of Bombyx mori silk fibroin by reducing the pH. Transmission electron microscopy, scanning electron microscopy, and dynamic light scattering were used to characterize the dilute solutions of silk fibroin in an aqueous environment, and provide direct visualization of the transformation of spherical micelles at pH 6.8 to nanofibrils at pH 4.8. This change in morphology occurred as a result of the stretching entropy due to the formation of $eta$-sheets, which was analyzed using circular dichroism spectroscopy. This study demonstrates the self-assembly of silk fibroin as a function of pH.