We investigated the relationship between the deformation of the molecular network of myosin and actin and the macroscopic actuator contraction. Although several bioactuators using actomyosin have been reported in the past, the relationship between the molecular-scale structure and the motion of actomyosin actuators remains largely unexplored. We stained for actin, myosin, and collagen, respectively, and observed the internal biomolecular structure of the actuator by fluorescence observation. We took time-lapse images of the contraction of fluorescently stained actuators and determined the molecular contraction ratio of actomyosin. Finally, the macro and micro contraction ratios of the actuators were compared and examined to understand the internal mechanism of the actomyosin-collagen bioactuator.