Tropomyosin molecules attach to the thin filament conjointly rather than separately, in a pattern indicating very high cooperativity. The equilibrium process drawing tropomyosins together on the actin filament can be measured by application of a linear lattice model to binding isotherm data and hypotheses on the mechanism of cooperativity can be tested. Each end of tropomyosin overlaps and attaches to the end of a neighboring tropomyosin, facilitating the formation of continuous tropomyosin strands, without gaps between neighboring molecules along the thin filament. Interestingly, the overlap complexes vary greatly in size and composition among tropomyosin isoforms, despite consistently cooperative binding to actin. Also, the tendency of tropomyosin to bind to actin cooperatively rather than randomly does not correlate with the strength of end-to-end binding. By implication, tropomyosin’s actin-binding cooperativity likely involves effects on the actin filament, as well as direct interactions between adjacent tropomyosins.