Myosins are a family of motor protein that creates directional movement by repeatedly binding to actin filaments. The structural transitions within the motor protein are tightly coupled to the actin-binding states and cyclic hydrolysis of ATP and release of the products (ADP and Pi). So far, X-ray crystal structures of actomyosin complex at its various states have not been solved. Thus, detailed structural transitions within the myosin and their relation to actin binding, ATP hydrolysis, and product release are yet to be determined. Recently, high-resolution maps of myosin II in rigor (Fujii & Namba 2017) and myosin V in strong ADP state (Wulf et al. 2016), both in association with actin filaments, have been solved by cryo-electron microscopy (cryo-EM). In the present work, we apply the Normal Mode Analysis on Elastic Network Model (ENM) and a structural perturbation method (Tehver et al. 2009) to determine the critical nodes in the network and try to construct an allosteric network between the converter, the actin-binding interface, and the nucleotide-binding pocket. Different ENMs are tested and compared in this work, to show how the density of nodes and choose of force constant will affect the results.