Elucidating conformational dynamics of glycans and their interactions with proteins: a multiscale simulation study

Abstract

Carbohydrates, alongside proteins, nucleic acids, and lipids, constitute one of the four primary categories of organic molecules in nature. The term carbohydrate is interchangeable with glycan, monosaccharide, or polysaccharide. The intricate diversity of carbohydrates in living organisms results from various characteristics, including the capacity of different sugar residues to create glycosidic bonds, the type of anomeric linkage, the presence or absence of branching, and their independence from any template. What adds to the fascination of glycans is their remarkable ability to encode biological information, distinct from the information encoded by the genome. Glycans are frequently encountered in conjunction with other molecules termed glycoconjugates, which are large molecules consisting of a carbohydrate linked to a non-carbohydrate moiety. These glycoconjugates may manifest as glycoproteins (where glycans are covalently bonded to proteins), glycolipids (molecules comprising a lipid and a carbohydrate component), and proteoglycans (core proteins with one or more extended chains of glycosaminoglycans or GAGs, attached). An understanding of the structure and function of glycoconjugates is essential for unraveling the complexities of cellular communication, development, and disease.