Myosin from silver carp was sonicated with varying power output (100, 150, 200 and 250W) for 3, 6, 9, and 12min. The changes in the structure and physicochemical properties of myosin were evaluated by dynamic light scattering, SDS-PAGE and some physicochemical indexes. The ultrasound treatments induced a significant conversion of myosin aggregates to smaller ones with a more uniform distribution, and obvious enhancement in solubility. The structure of myosin was also notably changed by sonication, with a decrease in Ca2+-ATPase activity and SH content, and an increase in surface hydrophobicity. Furthermore, SH groups were oxidized, leading to a decrease in reactive SH and total SH contents. SDS-PAGE analysis revealed that ultrasound could induce the degradation of myosin heavy chain and change the protein fraction of myosin. Collectively, the ultrasonic treatment of 100W for 3min showed slight influence on the SH content, S0-ANS, and electrophoretic patterns, and the extent of changes in myosin structure and physicochemical properties tended to increase with ultrasonic power and time. The integrated data indicate that ultrasonic treatment can facilitate the improvement of the solubility and dispersion of myosin, but the choice of a suitable ultrasonic condition to avoid oxidation and degradation of myosin is very important.