Almost all proteins on the cell surface and in body fluids, such as G protein-coupled receptors (GPCRs), sodium channels, cytokines, and hormones, are glycosylated [1]. In addition, many proteins, including GPCRs, undergo N-linked glycosylation under genetic control at regions involved in ligand binding. It is already well known that these glycans significantly affect the protein tertiary structure, protein dynamic behavior, and protein–protein interactions. However, the underlying mechanisms of these effects remain unclear. Similar phenomena can be observed in other important biological processes. For example, the histone code regulates interactions between histone proteins and DNA during transcription and replication. Moreover, epigenetic modifications such as DNA methylation have a major influence on transcription into RNA. Both the histone code and epigenetics are governed by complex biological systems, and a detailed understanding of these processes requires further fundamental research [2].