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"equatorial bond"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
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  • order of bond
    °áÇÕÂ÷¼ö(Ì¿ùêó¬â¦).
  • peptide bond
    ÆÕƼµå°áÇÕ
  • peptide bond
    ÆéŸÀ̵å°áÇÕ.
  • polar bond
    ±Ø¼º°áÇÕ(пàõÌ¿ùê).
  • semipolar bond
    ¹Ý±Ø¼º °áÇÕ(ÚâпàõÌ¿ùê).
  • triple bond
    »ïÁß°áÇÕ(¡­Ì¿ùê).
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  • isologous bond
    µ¿Á¾°áÇÕ(ÔÒðúÌ¿ùê)
  • isopeptide bond
    ¾ÆÀÌ¼ÒÆéŸÀ̵å°áÇÕ(Ì¿ùê)
  • localized bond
    ±¹¼Ò°áÇÕ(ÏÑá¶Ì¿ùê)
  • lyophobic bond
    ¼Ò¾×°áÇÕ(áÃäûÌ¿ùê)
  • noncovalent bond
    ºñ°øÀ¯ °áÇÕ(ÞªÍëêóÌ¿ùê)
  • nonpolar bond
    ¹«±Ø¼º°áÇÕ(ÙíпàõÌ¿ùê)
  • peptide bond
    ÆéŸÀÌµå °áÇÕ(Ì¿ùê)
  • phosphate bond energy
    Àλê°áÇÕ(×ò߫̿ùê) ¿¡³ÊÁö
  • phosphodiester bond
    Àλê(ìÝß«)ÀÌ(ì£)¿¡½ºÅÍ °áÇÕ(Ì¿ùê)
  • "3',5'-phosphodiester bond"
    3`5'-Àλê(ìÝß«)ÀÌ(ì£)¿¡½ºÅÍ °áÇÕ(Ì¿ùê)
  • pi bond
    ÆÄÀ̰áÇÕ(Ì¿ùê)
  • polar bond
    ±Ø¼º°áÇÕ(пàõÌ¿ùê)
  • secondary bond
    ÀÌÂ÷ °áÇÕ(ì£ó­Ì¿ùê)
  • semipolar bond
    ¹Ý±Ø¼º °áÇÕ(ÚâпàõÌ¿ùê)
  • triple bond
    »ïÁß °áÇÕ(ß²ñìÌ¿ùê)
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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&equiv;CH (acetylene).
(05 Mar 2000)
eupeptide bond A peptide bond between the alpha-carboxyl group of one amino acid and the alpha-amino group of another amino acid.
Compare: peptide bond, isopeptide bond.
(05 Mar 2000)
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