Many proteins form oligomers under physiological conditions, which can confer thermal stability, greater complexity in structural and functional activity. Understanding the mechanisms of assembly provide insight into protein evolution, providing a framework for how protein structures adapt to gain new function. Previously, due to computational limits, intrinsic dynamics, or vibrational signatures, have typically been modelled implicitly by considering the conformation of a participating protein subunit in isolation. Generally, it is assumed the isolated subunit is in a conformation which captures the implicit effect of the binding partner on the intrinsic dynamics, suggesting the influence of a partnering subunit is already integrated. However, this description lacks detailed information on the influence of critical contacts at the protein-protein interface. Since the binding of many proteins to their protein partners is tightly regulated via control of their relative intrinsic dynamics, investigation of the intrinsic dynamics of proteins is necessary for the comprehensive understanding of function. In this study, we examine the case of a protein family, pyrimidine synthesis attenuator PyrR1, to understand the effect of the binding partners in the stability of the tetramer vs. the dimer, and to uncover signals that link to their modulation via allostery. By partitioning the covariance matrices from elastic network models to obtain normal modes2, we found that explicitly modelling the partnering subunits revealed the influence of perturbations that extend from the tetrameric interface, that is not captured by modelling the subunits in isolation.