Glycoconjugate in the context of "Peptide"

Polysaccharides (/ˌpɒliˈsækəraɪd/; from Ancient Greek πολύς (polús) 'many, much' and σάκχαρ (sákkhar) 'sugar') are "Compounds consisting of a large number of monosaccharides linked glycosidically". They are the most abundant carbohydrates in food. Their structures range from linear to highly branched polymers. Examples include storage polysaccharides such as starch, glycogen, and galactogen and structural polysaccharides such as hemicellulose and chitin. The term "glycan" is synonymous with polysaccharide, but often glycans are discussed in the context of glycoconjugates, i.e. hybrids of polysaccharides and proteins or lipids.

Polysaccharides are often heterogeneous, containing slight modifications of the repeating unit. They may be amorphous (e.g. starch) or insoluble in water (e.g. cellulose).

The glycocalyx is a microscopic, hair-like coating which covers the outer surface of virtually all cells, and plays a critical role in most signalling between cells and their surrounding environments. It is composed of branching biomolecules like proteins and lipids sometimes longer than the cell's own diameter, with various sugars covalently bound to them at particular locations.

The glycocalyx (pl.: glycocalyces or glycocalyxes), also known as the pericellular matrix and cell coat, is an external organelle consisting of a layer of glycosylated biomolecules called glycoconjugates, such as glycoproteins and glycolipids. These are embedded in and extend outwards from the cell membranes of virtually all cells. Generally, the carbohydrate portion of the glycolipids found on the surface of plasma membranes helps these molecules contribute to cell–cell recognition, communication, and intercellular adhesion.

Mucins (/ˈmjuːsɪn/) are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most animals. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. They often take an inhibitory role. Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms and bone formation in vertebrates. They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer.

Although some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, most mucins are secreted as principal components of mucus by mucous membranes or are secreted to become a component of saliva.

Glycosylation is the reaction in which a carbohydrate (or 'glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction.

Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced: