| ISTU | isometric strength testing unit |
|---|---|
| LIS | laboratory information system; lateral intercellular space; left intercostal space; library informat... |
| LISS | low-ionic-strength saline |
| LS | lateral suspensor; left sacrum; left septum; left side; legally separated; leiomyosarcoma; length of... |
| mm | st muscle strength |
| high energy phosphate bond | See: high energy phosphates. (05 Mar 2000) |
|---|---|
| semipolar bond | A bond in which the two electrons shared by a pair of atoms belonged originally to only one of the atoms; often represented by a small arrow pointing toward the electron receiver; e.g., nitric acid, O(OH)N→O; phosphoric acid, (OH)3P→O. Synonym: coordinate covalent bond. (05 Mar 2000) |
| hydrogen bond | <chemistry> A weak electrostatic link between an electronegative atom (such asoxygen) and a hydrogen atom which is linked covalently to anotherelectronegative atom, hydrogen bonding is what makes water stick toitself. (09 Oct 1997) |
| hydrophobic bond | See: hydrophobic interaction. (05 Mar 2000) |
| sigma bond | <chemistry> A bond formed from the overlap of either two s-orbitals or two hybrid orbitals such as sp3 or sp2 orbitals. (09 Jan 1998) |
| single bond | A covalent bond resulting from the sharing of one pair of electrons; e.g., H3C-CH3 (ethane). (05 Mar 2000) |
| noncovalent bond | Bond in which electrons are not shared between atoms; e.g., electrostatic bond, hydrogen bond. (05 Mar 2000) |
| sulfur-sulfur bond isomerases | <enzyme> Enzymes that catalyze the transposition of a sulfur-sulfur bond. Registry number: EC 5.3.4 (12 Dec 1998) |
| disulfide bond | A single bond between two sulfurs; specifically, the -S-S- link binding two peptide chains (or different parts of one peptide chain); also occurs as part of the molecule of the amino acid, cystine, and is important as a structural determinant in many protein molecules, notably keratin, insulin, and oxytocin. A symmetric disulfide is R-S-S-R; R'-S-S-R is a mixed disulfide. (05 Mar 2000) |
| disulphide bond | <chemistry, molecular biology> The S S linkage. A linkage formed between the SH groups of two cysteine moieties either within or between peptide chains. Each cysteine then becomes a half cystine residue. S S linkages stabilise, but do not determine, secondary structure in proteins. They are easily disrupted by SH groups in an exchange reaction and are not present in cytosolic proteins (cytosol has a high concentration of glutathione that has a free SH residue). (18 Nov 1997) |
| double bond | <chemistry> A covalent bond resulting from the sharing of two pairs of electrons; e.g., H2C==CH2 (ethylene). (05 Mar 2000) |
| isopeptide bond | An amide linkage between a carboxyl group of one amino acid and an amino group of another amino acid in which at least one of these groups is not on the a-carbon of one of the amino acids; for example, the bond between the glutamyl residue and the cysteinyl residue of glutathione. Compare: peptide bond, eupeptide bond. (05 Mar 2000) |
| electrostatic bond | Bond between atoms or groups carrying opposite charges (or, in some cases, partial charges). Synonym: heteropolar bond, salt bridge. (05 Mar 2000) |
| energy-rich bond | See: high energy compounds. (05 Mar 2000) |
| triple bond | A covalent bond resulting from the sharing of three pairs of electrons; e.g., HC≡CH (acetylene). (05 Mar 2000) |