The present work investigated the effects of heat treament on the interactions of myofibrillar protein with fishy odor compounds. Four typical fishy odor compounds were selected and the myofibrillar protein-fishy odor compounds system were established. The changes in the structures of myofibrillar protein and binding capacity with volatile compouns during one-stage heating process of surimi were determined by UV spectra， fluorescence spectroscopy， Raman spectroscopy and head-space sampling combined with gas chromatography-mass spectrometry （HS-GC-MS） technology. The results showed that the turbidity， surface hydrophobicity and total sulfhydryl content of myofibrillar protein solution increased first and then decreased with the extension of heat treatment time（P<0.05）， and the endogenous fluorescence intensity of protein decreased gradually. Within 0-5 min of heating， the content of α-helix decreased significantly（P<0.05）， while the β-sheet and β-turn content increased obviously （P<0.05）. Subsequently， the content of α-helix increased and the β-sheet decreased when the heating time exceeded 5 min. The binding capacity of volatile aldehydes to myofibrillar protein was significantly influenced by the heating treatment. At the initial stage of heating， the structure of myofibrillar protein was unfolded and the binding ability with the aldehydes was significantly enhanced（P<0.05）. The binding capacity of hexanal， heptanal and nonanal reached the maximum at 5 min of heating， while that of octanal reached the maximum at 2 min. After that， the binding ability decreased significantly with the prolongation of heating time （P<0.05）.