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  2. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Their number and arrangement is called the secondary structure of the protein. Alpha helices are regular spirals stabilized by hydrogen bonds between the backbone CO group of one amino acid residue and the backbone NH group of the i+4 residue. The spiral has about 3.6 amino acids per turn, and the amino acid side chains stick out from the ...

  3. Glycosidic bond - Wikipedia

    en.wikipedia.org/wiki/Glycosidic_bond

    A substance containing a glycosidic bond is a glycoside. The term 'glycoside' is now extended to also cover compounds with bonds formed between hemiacetal (or hemiketal) groups of sugars and several chemical groups other than hydroxyls, such as -SR (thioglycosides), -SeR (selenoglycosides), -NR 1 R 2 (N-glycosides), or even -CR 1 R 2 R 3 (C ...

  4. Glycolipid - Wikipedia

    en.wikipedia.org/wiki/Glycolipid

    Glycolipid. Glycolipids are lipids with a carbohydrate attached by a glycosidic (covalent) bond. [1] Their role is to maintain the stability of the cell membrane and to facilitate cellular recognition, which is crucial to the immune response and in the connections that allow cells to connect to one another to form tissues. [2]

  5. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons. It often, but not always, involves some chemical bonding.

  6. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    A double bond between two given atoms consists of one σ and one π bond, and a triple bond is one σ and two π bonds. [8] Covalent bonds are also affected by the electronegativity of the connected atoms which determines the chemical polarity of the bond. Two atoms with equal electronegativity will make nonpolar covalent bonds such as H–H.

  7. Hydrolysis - Wikipedia

    en.wikipedia.org/wiki/Hydrolysis

    Monosaccharides can be linked together by glycosidic bonds, which can be cleaved by hydrolysis. Two, three, several or many monosaccharides thus linked form disaccharides, trisaccharides, oligosaccharides, or polysaccharides, respectively. Enzymes that hydrolyze glycosidic bonds are called "glycoside hydrolases" or "glycosidases".

  8. Glossary of cellular and molecular biology (M–Z) - Wikipedia

    en.wikipedia.org/wiki/Glossary_of_cellular_and...

    M phase See mitosis. macromolecule Any very large molecule composed of dozens, hundreds, or thousands of covalently bonded atoms, especially one with biological significance. . Many important biomolecules, such as nucleic acids and proteins, are polymers consisting of a repeated series of smaller monomers; others such as lipids and carbohydrates may not be polymeric but are nevertheless large ...

  9. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The two most common linkages in glycoproteins are N-linked and O-linked glycoproteins. [3] An N-linked glycoprotein has glycan bonds to the nitrogen containing an asparagine amino acid within the protein sequence. [4] An O-linked glycoprotein has the sugar is bonded to an oxygen atom of a serine or threonine amino acid in the protein. [4]