Allostery, the phenomenon where changes in one part of a protein influence distant regions, remains a crucial yet not fully understood aspect of protein function. To address this, we investigate allosteric mechanisms in purine nucleoside phosphorylases (PNPs), focusing on hexameric PNPs from prokaryotes like Helicobacter pylori. [1] Our project, ALOKOMP (Allosteric communication pathways in oligomeric enzymes), [2] employs innovative time-dependent diagrams to track protein movements, integrating static structures with the dynamic data from molecular dynamics simulations. Structural alignment and Ramachandran [3] angle analysis are performed to elucidate conformational changes, with novel time-dependent Ramachandran diagrams (Figure 1) revealing correlated movements of amino acids. Python visualization tools help in data analysis and presentation, highlighting potential allosteric communication hubs. This research enhances our understanding of PNP allostery and offers insights into enzyme dynamics.