Towards this aim, I apply and build upon two recently developed network analysis methodologies, MD-Sectors (Fabry, 2020;Lakhani, Thayer, Black, & Beveridge, 2020) and MD-END (Abramson, 2021), for analyzing pairwise residue networks generated from differential forms of biophysical interactions to the same allosteric model system, CRIB-Par6. In a synthesized analysis of both methodologies, I investigate the clustering, cohesiveness, and density of residue communities within these networks resulting from the decomposition of residues' pairwise covariances in motional (MD-Sectors) and non-bonded interaction energic (MD-END) interactions. I additionally develop a pairwise embedding error analysis that works upon the MD-END methodology to analyze the degree of energetic modulation of specific residues between networks that lead to their differential graph embeddings across different protein interactions. Through this combined approach, we hope to find complementary insight into how protein systems such as CRIB-Par6 may use different and potentially overlapping allosteric pathways to confer global and local changes to structure and function incident to protein-specific interactions. In the utility and development of these methodologies we demonstrate that with the significance of conformational dynamics to binding interactions, the role of electrostatically-mediated energetic signalling is equally important towards a comprehensive view of allosteric signalling.