Effective usage of proteins as structural components in food systems requires an understanding of the mechanisms and interactions responsible for network formation. Network characteristics can be evaluated by examining physicochemical properties, microstructure and rheological properties. Microscopy and rheology have been particularly valuable in elucidating network forming behavior for globular proteins. Current literature indicates that heat-induced network formation of globular proteins involves partial unfolding of the protein followed by the interaction of the resulting globular structures. The rate and degree of interaction for these structures is controlled by the electrostatic repulsion within the system. Interactions responsible for protein-protein associations include hydrogen bonding, hydrophobic interactions and for some proteins, electrostatic attractions and/or disulfide bonds. The characteristics of the resulting network will depend on the balance between attractive and repulsive forces as well as the relative contributions of the various interactions.