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Domain I (residues 1–27 and 383–414) forms a three-stranded anti-parallel β-sheet. This domain contains two disulfide bridges that are necessary for correct folding, as well as a glycosylated residue (Asn19) that is required for catalytic activity in vivo.
For instance, some proteins do not fold correctly unless they are glycosylated. [2] In other cases, proteins are not stable unless they contain oligosaccharides linked at the amide nitrogen of certain asparagine residues. The influence of glycosylation on the folding and stability of glycoprotein is twofold. Firstly, the highly soluble glycans ...
Proteoglycans are proteins [1] that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein " with one or more covalently attached glycosaminoglycan (GAG) chain(s). [ 2 ] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate ...
One of the first and only examples of O-glycosylation on tyrosine, rather than on serine or threonine residues, is the addition of glucose to a tyrosine residue in glycogenin. [7] Glycogenin is a glycosyltransferase that initiates the conversion of glucose to glycogen, present in muscle and liver cells. [27]
The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...
P-gp is a 170 kDa transmembrane glycoprotein, which includes 10–15 kDa of N-terminal glycosylation.The N-terminal half of the protein contains six transmembrane helixes, followed by a large cytoplasmic domain with an ATP-binding site, and then a second section with six transmembrane helixes and an ATP-binding domain that shows over 65% of amino acid similarity with the first half of the ...
They arise by the condensation of 3-deoxyglucosone with the guanidine group of an arginine residue. [7] Glycations occur mainly in the bloodstream to a small proportion of the absorbed simple sugars: glucose, fructose, and galactose. It appears that fructose has approximately ten times the glycation activity of glucose, the primary body fuel. [8]
The resulting GPI-anchored proteins play key roles in a wide variety of biological processes. [1] GPI is composed of a phosphatidylinositol group linked through a carbohydrate -containing linker ( glucosamine and mannose glycosidically bound to the inositol residue) and via an ethanolamine phosphate (EtNP) bridge to the C-terminal amino acid of ...