The mechanism of the interaction bighead carp myosin binding characteristic fishy odor compounds was illustrated by establishing a system of myosin-fishy odor compounds. The interaction of myosin with fishy odor compounds were explored by HS-GC-MS， molecular simulation， DSC， Raman spectroscopy， etc. The results showed that the binding ability of myosin with six fishy odor compounds increased significantly with the increase of carbon chain length and unsaturation degree. In addition， the binding ability of 1-octen-3-ol was significantly lower than that of aldehydes. The existence of odor compounds unfolded the molecular structure of myosin and caused the transformation of α-helix to β-sheet and β-turn. Meanwhile， the surface hydrophobicity of myosin， total sulfhydryl groups and active sulfhydryl group increased， while the absolute value of Zeta potential and thermal stability of myosin decreased. Moreover， the effect of aldehydes on the structure of myosin was significantly higher than that of alcohols. The interaction forces between selected fishy substances and myosin were mainly hydrophobic interaction， hydrogen bonding and covalent bonding.