According to our hypothesis of the peptide bond SASA of the cleavage sites, glycoforms whose scissile bonds are less solvent-exposed should have higher proteolytic stability. To examine this hypothesis, we plotted the 𝛼-chymotrypsin half-life measured in the experimental work against the SASA value of each of the two scissile bonds, including the one between residues B25 and B26 (upper panel of Figure ) and the one between residues B26 and B27 (lower panel of Figure ). Ideally, a good computational metric should be able to reproduce consistent results as compared to the work by Guan et al. , leading to a Kendall's tau correlation coefficient close to -1. A good metric should also be immune to the starting model bias, including the bias from wild-type models resolved using different methods or under different conditions, or the bias solely from different protonation states of the histidine residues.