Each step of glycolysis is characterized by a specific enzyme that acts to catalyze a given reaction. Unique amongst these reactions is the enolase-catalyzed transformation of 2-phosphoglycerate into phosphoenolpyruvate by dehydration. Studies have shown enolase to have a dimeric structure in all eukaryotes whereas the enzyme has been observed to possess an octameric structure in some extreme thermophile prokaryotes. Though a definitive determination of molecular architecture has not been made, anecdotal evidence seems to indicate that a tetrameric association of dimers is the most likely native form. This study has produced computational models for three mutation/deletion variants of the enzyme HL–S1 loop, which has been proposed as a contact point between the dimer subunits. Examination of these models with a dielectric constant of 40 has indicated a rapid deterioration of protein conformation; however, dielectric constants of 0 and 80 maintained overall structure. The study also showed that the deletion of residues 135–138 did not completely eliminate the alpha helix that was hypothesized to inhibit octameric structure.