¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"dative 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.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 9 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • multiple bond
    ´ÙÁß°áÇÕ(ÒýñìÌ¿ùê).
  • nonpolar bond
    ¹«±Ø¼º °áÇÕ(~Ì¿ùê).
  • nonpolar bond
    ºñ±Ø¼º °áÇÕ(~Ì¿ùê).
  • 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).
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • electron pair bond
    ÀüÀÚ½Ö °áÇÕ(ï³í­äªÌ¿ùê)
  • electrostatic bond
    Á¤Àü±â °áÇÕ(ð¡ï³Ñ¨Ì¿ùê)
  • energy-rich bond
    ºÎ(Ý£)¿¡³ÊÁö °áÇÕ(Ì¿ùê)
  • equatorial bond
    ¼öÆò¹æÇâ °áÇÕ (â©øÁÛ°ú¾Ì¿ùê)
  • exocyclic bond
    °í¸®¹Û °áÇÕ(Ì¿ùê)
  • glycosidic bond
    ±Û¶óÀÌÄÚ»çÀÌµå °áÇÕ(Ì¿ùê)
  • heterologous bond
    À̺ÎÀ§ °áÇÕ(ì¶Ý»êÈÌ¿ùê)
  • high-energy bond
    °í(ÍÔ)¿¡³ÊÁö °áÇÕ(Ì¿ùê)
  • hydrogen bond
    ¼ö¼Ò °áÇÕ(â©áÈÌ¿ùê)
  • hydrophobic bond
    ¼Ò¼ö °áÇÕ(áÂâ©Ì¿ùê)
  • ionic bond
    À̿°áÇÕ(Ì¿ùê)
  • isoelectronic bond
    µîÀüÀÚ°áÇÕ(Ôõï³í­Ì¿ùê)
  • isologous bond
    µ¿Á¾°áÇÕ(ÔÒðúÌ¿ùê)
  • isopeptide bond
    ¾ÆÀÌ¼ÒÆéŸÀ̵å°áÇÕ(Ì¿ùê)
  • localized bond
    ±¹¼Ò°áÇÕ(ÏÑá¶Ì¿ùê)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
coordinate covalent 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)
covalent bond A bond between two or more atoms that is provided by electrons that travel between the atoms' nuclei, holding them together but keeping them a stable distance apart.
(09 Oct 1997)
heteropolar bond Bond between atoms or groups carrying opposite charges (or, in some cases, partial charges).
Synonym: heteropolar bond, salt bridge.
(05 Mar 2000)
high energy bond <chemistry> Chemical bonds that release more than 25kJ/mol on hydrolysis: their importance is that the energy can be used to transfer the hydrolysed residue to another compound. The risk in using the term is that students may think the bond itself is different in some way, whereas it is the compound that matters. Hydrolysis of creatine phosphate yields 42.7kJ/mol, of phosphoenolpyruvate, 53.2, ATP to ADP, 30.5: the latter is important because it shows that energetically the hydrolysis of creatine phosphate will suffice to reconstitute ATP, hence the use of creatine phosphate in muscle.
(18 Nov 1997)
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&rarr;O; phosphoric acid, (OH)3P&rarr;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)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 14 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • fiduciary bond
    ¼öŹÀÚ º¸Áõ
  • general obligation bond
    ÀÏ¹Ý º¸ÁõÁ¦(¿ø±Ý°ú ÀÌÀÚ ÁöºÒÀÌ º¸ÁõµÇ¾î ÀÖ´Â Áö¹æÁ¤ºÎä)
  • government bond
    ±¹Ã¤
  • ionic bond
    (È­)À̿ °áÇÕ
  • pair bond
    ¾Ï¼ö 1´ë 1ÀÇ °ü°è 
  • performance bond
    °è¾à ÀÌÇà º¸Áõ¿ë ±ÝÀü 乫 Áõ¼­
  • preference bond
    ¿ì¼± Á¤ºÎ °øÃ¤
  • premium (savings) bond
    ÇÒÁõ±ÝÀÌ ºÙÀº ä±Ç
  • premium on bond
    ȸ»çä ¹ßÇà Â÷±Ý
  • purchasing power bond
    ±¸¸Å·Â ä±Ç(±¸¸Å·ÂÀ» ³ªÅ¸³»´Â Áö¼ö¿¡ ¿¬µ¿½ÃÄÑ ÀÌÀÚ,»êȯ¾×À» º¯µ¿ÄÉ ÇÏ´Â °Í)
  • ransom bill(bond)
    ³ªÆ÷ ¼±¹ÚÀÇ ¹è»ó Áõ¼­
  • registered bond
    ±â¸í °øÃ¤(¼ÒÀ¯ÀÚÀÇ À̸§ÀÌ ÀûÈù)
  • revenue bond
    ¼¼ÀԴ㺸ä
  • savings bond
    ÀúÃàä±Ç
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
ÅëÇÕ°Ë»ö ¿Ï·á