By using protein-glutaminase (PG) deamidation, thermo-reversible gel of pork myofibrillar protein (PMP) can be prepared. This study aims to reveal the connection between PMP thermo-reversible gel and the coiled-coil. The research explores how the water-holding capacity and reversibility of these gels improve with increased deamidation time. At a deamidation duration of 4 h, the gel strength reaches its peak. Moreover, PG deamidation significantly enhances the α-helix content to over 60 %. This change boosts the likelihood of α-helix interactions while increasing coiled helix content. Notably, the interference experiment of trifluoroethanol suggests that a high concentration of coiled coils is essential for imparting reversible properties to the deamidated myofibrillar protein gel. This research contributes to the advancement of protein micro-modification in the custom manufacturing of muscle protein-based soft meal products.