“…Many proteins undergo co-or post-translational modifications, including phosphorylation, acetylation, and glycosylation to fulfill their functions (Walsh and Jefferis, 2006;Carubbi et al, 2019). It is estimated that glycosylation modifications are associated with approximately 50% of human proteins (Clerc et al, 2016;Oliveira-Ferrer et al, 2017) and 30% of approved biopharmaceutical proteins (Zou et al, 2020), which are critical for important biological processes in living systems, such as cell's adhesion, recognition, targeting, and differentiation (Varki, 2017;Bhat et al, 2019). Despite the importance of glycosylations, rigorous evaluation of the relationship between the precise structure and biological function of glycoproteins is complicated by the structural heterogeneity of the oligosaccharides in biological organisms, and the difficulty to obtain sufficient amounts of structure-defined glycoproteins with single glycoform from natural sources (Park et al, 2009).…”