Changing attitudes towards fish products and the resultant increase in consumption has promoted interest in gelled comminuted fish products, particularly those made from previously underutilized species. Species-dependent variability in gelation and the need to maximize raw material utilization has prompted numerous studies aimed at exploiting the role of muscle proteins in this process. This research has resulted in the formulation of a mechanism to explain the phenomenon of gelation in fish proteins. According to this hypothesis, the myosin molecule, shown to be the major protein involved in gelation, aggregates at certain regions and by various forms of interaction, the degree of which are species specific. Initially, a three-dimensional network is established during the setting process through linkages in the tail portion of the molecule via hydrophobic interactions. Subsequent processes involve continued tail-tail connections, however, disulfide linkages between head segments of myosin assume a prominent role in the final stages of gelation. Other forms of bonding and additional proteins are thought to be actively involved throughout the gelling process but as yet there is insufficient evidence to confirm their exact functions.