Talin is an important linking between integrin and the actin cytoskeleton. In the process of signal transduction, talin play a critical role in the bidirectional signal transfer. In this paper, we analyze the motion modes of talin rod domain with the Gaussian network model. The results show that the two free terminals move in a negative correlated way, and this large-scale conformational change trend rest with the topological characteristics of the structure. For the peaks of the fast modes, it corresponds to some residues, and these residues are important to the stability of the structure. They may also act as key residues when they talin interacted with integrin or other signaling molecules. As an inherent feature of the structure, these motion modes are determined by the topology character of the structure. These results can provide a better understanding of the motion trend of talin in the process of signal transfer.