Allostery plays a crucial role in enzyme regulation, yet the underlying communication pathways often remain hidden within the complexity of protein dynamics. In this work, we investigated purine nucleoside phosphorylase (PNP) from Helicobacter pylori [1] using microsecond-scale molecular dynamics simulations combined with advanced data analysis. We developed a method, MDavocado, [2] which follows time-dependent φ/ψ backbone angle variations for each amino acid, providing compact visualizations of conformational transitions throughout the simulation. This approach enables identification of dynamically active residues and regions involved in coordinated conformational changes. By applying circular correlation analysis and graph theory, we mapped residue–residue communication networks that propagate structural changes across the enzyme. The detected pathways are primarily located at dimer interfaces, within the central cavity, and near the active sites, suggesting potential routes of allosteric signal transmission. Our results provide new insights into the dynamic behavior and internal communication of PNP, demonstrating how combining molecular dynamics with network analysis can uncover the structural basis of allosteric regulation.