Previous experimental studies of 𝛼-chymotrypsin complexes revealed an invariant feature that the polypeptide binding sites of 𝛼-chymotrypsin formed a short antiparallel 𝛽-sheet with the backbone atoms of the P1-P3 sites of the substrate. In the case of insulin as the substrate, considering the P1 to P3 sites of both important cleavage sites (PheB25 and TyrB26) leads to residues including ArgB22, GlyB23, PheB24, and PheB25. As such, we hypothesized that glycoforms whose ArgB22 to PheB25 residues had lower 𝛽sheet propensity would destabilize the transition state in the protease-substrate binding event, hence decreasing the proteolytic susceptibility. This assumption also stemmed from the fact that drastic structural re-orientations or even secondary structure transformations of the insulin substrate cost free energy and disfavored proteolysis accordingly. To evaluate the 𝛽-sheet propensity of these sites, we calculated the 𝜓 and 𝜙 angles of the residues. We then used MDAnalysis to locate all the frames in a Ramachandran plot and defined the 𝛽-sheet propensity as the fraction of the points in the 𝛽-sheet region defined by Lovell et al. Again, for each glycoform, we report the fractions averaged across different wild-type bases, with the uncertainty reported as the standard deviation of the mean over simulations with the five different initial structures. Finally, the 𝛼-chymotrypsin half-life was plotted against these averaged 𝛽-sheet fractions in a correlation plot, where the Kendall's tau correlation coefficient (𝜏) and its uncertainty were determined using the bootstrap method described in section 2.3. The Ramachandran plot of each of the 4 residues of interest of each glycoform can be found in our GitHub repository. Additionally, in the supporting information (Figures and), we examined the correlations between any two of the four measures (B22-B25) of the 𝛽-sheet propensity metric and the correlations between any SASA measure in Metric 1 or Metric 2 and any 𝛽-sheet propensity measure in Metric 3.