Before revision:  To this end , we synthesize a biomimetic active nematic liquid crystal from long semi-flexible actin filaments driven out-of-equilibrium by myosin motor activity. We identify new actomyosin interactions that govern the dynamic architecture and mechanical response of the network to active stresses. These responses include dynamic steady states, in which myosin induces transverse plucking of actin filaments, whose curvatures show anomalous and strongly coupled fluctuations across a broad spectrum of filament bending modes. These fluctuations break detailed balance, yet promote dynamic stability in a network predisposed to instabilities. Furthermore, the actomyosin interactions that maintain dynamic stability are fundamentally distinct from those that drive contractile flows of actomyosin networks.
After revision:  To this end , we synthesize an actomyosin material in vitro whose active stress content can tune the network from stable to contractile. Each increment in activity determines a characteristic spectrum of actin filament fluctuations which is used to calculate the total mechanical work and the production of entropy in the material. We find that the balance of work and entropy does not increase monotonically and, surprisingly, the entropy production rate is maximized in the non-contractile, stable state. Our study provides evidence that the origins of system entropy production and activity-dependent dissipation arise from disorder in the molecular interactions between actin and myosin