Protein network formation is the primary determinant of structure, texture, and cooking quality in wheat-based foods. While gluten proteins provide the structural backbone of dough systems, globular proteins from egg, soy, and whey are frequently incorporated into formulations, giving rise to complex co-protein interactions. These interactions influence thermal denaturation, sulfhydryl–disulfide exchange reactions, hydrophobic aggregation, and phase behaviour. The extent and kinetics of protein polymerization determine whether composite systems exhibit synergistic reinforcement or structural weakening. In noodle systems, optimal protein network formation must accommodate starch gelatinization while maintaining structural integrity during cooking. This review synthesizes current understanding of gluten architecture, globular protein reactivity, intermolecular bonding mechanisms, and their collective impact on noodle texture and cooking stability. Emphasis is placed on balancing covalent and non-covalent interactions to achieve superior product quality. Insights into molecular compatibility and redox control provide opportunities for ingredient substitution, texture optimization, and development of sustainable wheat-based foods.