These results suggest that the dimer occlusion metric is independent of the initial model of human insulin. Since we cannot include a wild type in this analysis, there is no negative control for each glycoform set nor is there a way to predict percentage dimerization relative to wild type. But despite those drawbacks, this metric allows us to statistically differentiate results between glycoforms and the results are consistent with experimental data, and supports our hypothesis. The glycan-dimer occlusion metric, therefore, might be a useful predictor of dimerization propensity. Interestingly, the occlusion data suggests a unifying theme in glycan placement which might preclude dimerization: glycans that are large and those that are attached close to the dimer interface, especially residues ThrB27 and ThrB30.