To assess dimerization propensity, we examined glycan occlusion of the dimer interface. This metric was consistent with the limited experimental data for dimerization and is free from starting model bias. There is no ability to include a wild-type model for comparison, which is a drawback of this metric. However, this metric showed clear, statistical differences between glycoforms with and without occlusion which translates to predictive differences in dimerization potential and is independent of starting model. Additionally, this metric suggests a generalizable glycosylation scheme that might preclude dimerization: large glycans and those attached near the dimerization interface (ThrB27, ThrB30).