This study aimed to investigate the molecular interactions of silver carp myosin and three common plant polyphenols （EGCG， kaempferol， and quercetin） by protein homology modeling and molecular docking techniques. Moreover， the effects of EGCG binding to the myosin on entire structure of myofibrillar protein and its aggregation behavior were further explored， and the effect of tea polyphenol supplementation on microwave heating-induced gel formation of myofibrillar protein from silver carp was finally determined. The results showed that EGCG， kaempferol， and quercetin had the strong capacities to bind with myosin. Among them， EGCG had the greatest binding ability with the lowest docking energy， and the main interaction was noncovalent interaction including hydrogen bond and hydrophobic interaction. This interaction altered the secondary structure of myofibrillar protein， which reduced α-helix content， but increased β-turn and random coil contents， leading to a more unfolded structure of protein and its potential gel formation induced by high temperature. Furthermore， microwave heating contributed to the improved gel properties of myofibrillar protein as compared with water bath heating. Indeed， addition of 0.125-1 mg/mL EGCG could further improve the properties of microwave heating-induced myofibrillar protein gel. The beneficial effects of EGCG reached the maximum when the addition amount was 0.5 mg/mL， and the deformation and gel strength were increased by 59.9% and 89.8%， respectively. Therefore， the addition of EGCG and microwave heating could improve the gel properties of myofibrillar protein from sliver carp， and its mechanism was possible to be structure alteration and aggregation behavior of myofibrillar protein stimulated by interaction of EGCG with myosin. Our results may provide experimental and theoretical basis for improving the quality of surimi products of freshwater fish.