We examined four metrics based on two overarching hypotheses for proteolytic stability. The first is that the glycan could sterically hinder the scissile bonds or part of the binding sites, especially the P1 site, to prevent proteolysis, while the second is that the existence of the glycan disfavors configurations required for proteolytic degradation. From the first hypothesis, we derived two metrics, the SASA of the scissile bonds and the P1 sites. Both metrics were found partly predictive for assessing the proteolytic stability. Based on the second hypothesis, we examined 𝛽-sheet propensity of the P1-P3 region and the existence of glycaninvolved hydrogen bonds that compete with the hydrogen-bonding network present in 𝛼-chymotrypsin binding. The 𝛽-sheet propensity generally was not well correlated with proteolytic stability. The only residue whose 𝛽-sheet propensity suggested moderate predictiveness had excessively large error bars, making the metric less useful. Notably, the involvement of only a few atoms in the calculation naturally makes these 3 metrics relatively uncertain and less valuable. While the first 3 metrics are somewhat predictive or not predictive, long-lasting, stable glycan-involved hydrogen bonds, especially the ones involving residues PheB24 and ThrB27, were highly predictive in enhancing the proteolytic stability and independent initial wild-type model. In particular, using glycosylation site ThrB27 is more likely to form hydrogen bonds with ThrB27 and PheB24 due to spatial proximity.