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Two tyrosines separated by a single amino acid, typically valine or another tyrosine, form a short intra-molecular diphenylether crosslink. [11] This can be crosslinked further by the enzyme extensin peroxidase [12] [13] [14] to form an inter-molecular bridge between extensin molecules and thus form networks and sheets.
Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Additionally, structural proteins (1-5%) are found in most plant cell walls; they are classified as hydroxyproline-rich glycoproteins (HRGP), arabinogalactan proteins (AGP), glycine-rich proteins (GRPs), and proline-rich proteins (PRPs). Each class of glycoprotein is defined by a characteristic, highly repetitive protein sequence.
Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification .
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
Glycoconjugates are very important compounds in biology and consist of many different categories such as glycoproteins, glycopeptides, peptidoglycans, glycolipids, glycosides, and lipopolysaccharides. They are involved in cell–cell interactions, including cell–cell recognition; in cell–matrix interactions; and in detoxification processes.
O-linked glycans attached to the hydroxyl oxygen of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline side-chains, or to oxygens on lipids such as ceramide. Phosphoglycans linked through the phosphate of a phosphoserine. C-linked glycans, a rare form of glycosylation where a sugar is added to a carbon on a tryptophan side-chain.
To answer this question one should know the different and important functions of glycans. The following are some of those functions: Glycoproteins and Glycolipids found on the cell surface play a critical role in bacterial and viral recognition. They are involved in cellular signaling pathways and modulate cell function.