Explicit water atomistic molecular dynamics simulations (200 ns, ∼330,000 atoms) were performed to study the effects of galactosylation in the Fc domain of immunoglobulin G1. Two glycoforms were simulated to observe changes in protein-carbohydrate interactions and carbohydrate structure. A high degree of flexibility was observed in the small hinge region of the protein, while large domains remained stable. The hinge region flexibility allowed both translation and rotation of the domains relative to each other, resulting in a large number of possible conformations available. The distributions of rotational orientations between the Fab1 and Fab2 domains showed that while these domains are able to orient themselves rather freely pointing in space they rotated in unison to remain rotationally oriented at specific angles. Additionally, removing specific terminal galactose residues increased the mobility of the carbohydrate, resulting in different protein-carbohydrate interactions. Glycosylation has been suggested as a route to improve the aggregation resistance of monoclonal antibodies for therapeutic treatments to aid the immune system. The results presented here may provide insight into the search for IgG molecules with increased aggregation resistance to be used as monoclonal antibodies.