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  2. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    All cells are coated in either glycoproteins or glycolipids, both of which help determine cell types. [7] Lectins, or proteins that bind carbohydrates, can recognize specific oligosaccharides and provide useful information for cell recognition based on oligosaccharide binding. [citation needed]

  3. OB-fold - Wikipedia

    en.wikipedia.org/wiki/OB-fold

    Binding site location: In some proteins, the binding sites are located on the side surface of the β-barrel where three loops come together, in such a way they are partially wrapped by the binding partner. In others, the binding cleft at the side of the barrel opposite to the helix functions as binding site.

  4. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    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 ...

  5. Glycolipid - Wikipedia

    en.wikipedia.org/wiki/Glycolipid

    The saccharide of the glycolipid will bind to a specific complementary carbohydrate or to a lectin (carbohydrate-binding protein), of a neighboring cell. The interaction of these cell surface markers is the basis of cell recognitions, and initiates cellular responses that contribute to activities such as regulation, growth, and apoptosis. [7]

  6. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The oligosaccharide chains also change the solubility and polarity of the proteins that they are bonded to. [4] For example, if the oligosaccharide chains are negatively charged, with enough density around the protein, they can repulse proteolytic enzymes away from the bonded protein. [4]

  7. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. [2] Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6]

  8. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. [1] The binding partner of the macromolecule is often referred to as a ligand . [ 2 ]

  9. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised.