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2004-04-29 22:45:17 | Hit : 54492 | Vote : 8758 |
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Chapter 5. The structure and function of macromolecles |
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¡à Macromolecule
- polymer : bond¿¡ ÀÇÇØ ¿¬°áµÈ ¸¹Àº identical Çϰųª ºñ½ÁÇÑ building blocks·Î ±¸¼ºµÈ large molecule
- monomer : polymerÀÇ building blockÀ¸·Î¼ Á¦°øÇÏ´Â subunit
- condensation reaction (= dehydration reaction)
- Hydrolysis : polymer°¡ monomer·Î dissociate µÇ´Â °Í ; Hydro(water) + lysis(break)
¡à carbohydrates
- »ýü ³» ¸ðµç ź¼Ò¿¡´Â Àû¾îµµ ÇϳªÀÇ - OH groupÀ» °¡Áö°í ÀÖ´Ù.
- »ýü ³» ÃÖ¼Ò carbonÀÇ ¼ö´Â 3°³ÀÌ´Ù.
¨ç monosaccharides
cellÀÇ major nutrients. ƯÈ÷ glucose
- cellular workÀÇ major fuel
- small organic molecules(amino acid, fatty acid)ÀÇ ´Ù¸¥ typeÀÇ synthesis¸¦ À§ÇÑ raw material·Î¼ carbon skeletonÀ» Á¦°ø
- glucose linear form¿¡¼ ring formÀÇ Çü¼º
- °¡´ÉÇÑ µÎ°³ÀÇ glucose forms : ¥á form of glucos and ¥â form of glucose
¨è Disaccharides
µÎ monosaccharides »çÀÌ¿¡ Çü¼ºµÈ covalent bondÀÎ glycosidic linkage¿¡ ÀÇÇØ ¿¬°áµÈ µÎ°³ÀÇ monosaccharides·Î ±¸¼ºµÈ double sugar
¨é polysaccharides
¼ö ¸¹Àº monosaccharides. ¼·Î linkµÇ¾î polymer¸¦ Çü¼ºÇÑ macromolecule.
- ±â´É
¨± storage polysaccharide
©Í starch
- ½Ä¹°ÀÇ storage polysaccharide
- glucose monomer·Î¸¸ ±¸¼ºµÈ polymer (1,4 - linkage)
- helical shape
~ amylose : unbranched simplest form of starch
~ amylopectin : branched complex form polymer of starch
- plastid ¶ó´Â cellular structure »çÀÌ¿¡ granule·Î¼ ÀúÀå
©Î glycogen
- animalÀÇ storage polysaccharide
- plantÀÇ amylopectinº¸´Ù ´õ branched µÈ glucoseÀÇ polymer
- liver¿Í muscle cell¿¡ ÀúÀå
¨² structural polysaccharides
©Í cellulose
plant cellÀ» °¨½Î´Â tough wallÀÇ major component
©Î chitin
°ïÃæ·ù¿¡¼ ¿ÜÇÇ·Î »ç¿ëÇÏ´Â carbohydrate¿¡ ÀÇÇÑ structural polysaccharide ¡æ exoskeletonÀ» ¸¸µë
¡à Lipids
hydrophobic behavior ¡æ lipidÀÇ molecular structureÀÇ ±âº»À» Á¦°ø
- insoluble in water
- soluble in nonpolar solvent
¨ç Fats
large moleculeÀÌÁö¸¸ polymer´Â ¾Æ´Ï´Ù.
fat = glycerol + fatty acids
- saturated fatty acid : tailÀ» ±¸¼ºÇÏ´Â carbon atom »çÀÌ¿¡ double bond°¡ ¾ø´Â °Í. melting point°¡ ³ô´Ù (»ó¿Â¿¡¼ ¾ÈÁ¤ÈµÇ¾î °íü) ¡ç ÃÎÃÎÇÑ ±¸Á¶¿©¼ ±× ±¸Á¶¸¦ Ç®±â°¡ Èûµé´Ù.
- unsaturated fatty acid : tailÀ» ±¸¼ºÇÏ´Â carbon atom »çÀÌ¿¡ ÇÑ°³ ÀÌ»óÀÇ double bond°¡ ÀÖ´Â °Í. melting point°¡ ³·´Ù (»ó¿Â¿¡¼ ¾×ü) ¡ç ÃÎÃÎÇÑ ±¸Á¶°¡ ¾Æ´Ï¿©¼ ±× ±¸Á¶¸¦ Ç®±â°¡ ½±´Ù.
- animal fat : double bond°¡ ¾ø´Â saturated fatty acidÀÌ´Ù.
- plant fat : double bodn°¡ Çϳª ÀÌ»óÀÎ unsaturated fatty acidÀÌ´Ù. »ó¿Â¿¡¼ ¾×üÀÎ oil »óÅ ¡ç double bondÀÇ kink°¡ moleculeÀÇ room temperature¿¡¼ solidifyÇϱâ ÃæºÐÇϵµ·Ï °¡±õ°Ô ¸ðÀÌ´Â °ÍÀ» ¸·¾Æ¼ ±×·¸´Ù.
cf. hydrogenase·Î hydrogenÀ» Ãß°¡ÇØÁÖ¸é saturated plant fatÀ¸·Î º¯È¯ÀÌ °¡´ÉÇÏ¿© °íÇü»óÅÂÀÎ fatÀ» ¸¸µé ¼ö ÀÖ´Ù.
- saturated fat¿¡ ÀÇÇØ »ý±â´Â º´
atheroclerosis¶ó´Â human cardiovascular disease¸¦ À¯¹ßÇÑ´Ù. ¡ç saturated fatÀÌ plaque¶ó´Â deposits¸¦ Çü¼ºÇÏ¿© blood besselsÀÇ internal liningÀ» À̲ø¾î blood flow¸¦ °¡·Î¸·°í vesselsÀÇ resilience¸¦ ÁÙÀδÙ.
- fatsÀÇ function in life
©¿ energy storage : polysacchariedeÀÇ µÎ¹èÀÇ ¿¡³ÊÁö¸¦ ³½´Ù.
©À cushion ¿ªÇÒ : adipose tissue´Â kidney °°Àº vital organÀÇ skinÀ§¿¡ fat layer¸¦ Çü¼ºÇÏ¿© body¸¦ º¸È£ÇÑ´Ù.
¨è Phospolipids
- micelleÀ» Çü¼ºÇÑ´Ù. ex. ¼¼Å¹ ¼¼Á¦¿¡¼ ¶§¸¦ ¾ø¾Ö´Â ¿ø¸®Á¦°ø
- cell membraneÀÇ ÁÖ¿ä component
¨é Steroids
4°³ÀÇ ¼·Î ¿¬¼ÓÀûÀ¸·Î ¿¬°áµÈ carbon skeleton¿¡ ´Ù¾çÇÑ functional groupÀÌ ºÙ´Â ±¸Á¶
- cholesterol : animal cellÀÇ membrane¿¡ °øÅëÀû component. ´Ù¸¥ steroidÀÇ precursor
¡à Protein
- structural proteins : support
ex. silk fiber ¡æ °Å¹ÌÁÙ, collagen, elastin ¡æ animal connective tissue¿¡¼ fibrous framework, keratin ¡æ hair, horns, feater µî
- storage proteins : amino acidÀÇ ÀúÀå
ex. ovalbumin ¡æ °è¶õ ÈòÀÚ ; embryo ¼ºÀåÀ» À§ÇÑ amino acidÀÇ source, casein ¡æ milk, body mammalÀ» À§ÇÑ amino acidÀÇ major source
- transport proteins : ´Ù¸¥ substanceÀÇ À̵¿
ex. Hemoglobin
- Recerptor proteins : chemical stilmuli¿¡ ´ëÇÑ cellÀÇ ¹ÝÀÀ
- Contractile proteins : movement
ex. actin, myosin ¡æ muscleÀÇ movement¿¡ ¹ÝÀÀ, contractile protein ¡æ cilla, flagella
- Defensive proteins
ex. antibody
- Enzymatic proteins : chemical reactionÀÇ selective acceleration
ex. digetive enzyme
¡à Polypeptide
- amino acids : 20 Á¾·ù°¡ ÀÖ´Ù.
- condensation of amino acid for forming polypeptide
¡à proteinÀÇ specific conformation
- functional proteinÀº ´ÜÁö polypeptide chainÀÌ ¾Æ´Ï´Ù. Çϳª³ª ±× ÀÌ»óÀÇ polypeptidies°¡ Á¤¹ÐÇÏ°Ô twisted, folded, coiledµÇ¾î unique shapeÀÇ moleculeÀÌ µÈ´Ù.
- polypeptideÀÇ amino acid sequence¿¡ ±× ÃÖÁ¾ proteinÀÇ ¸ð¾ç¿¡ ´ëÇÑ Á¤º¸°¡ µé¾îÀÖÀ¸¸ç, ÀÌ Á¤º¸·Î proteinÀÌ ÃëÇÒ 3Â÷¿øÀÇ ±¸Á¶°¡ °áÁ¤µÈ´Ù.
- proteinÀÇ specific conformationÀº proteinÀÌ ¾î¶² ÀÏÀ» ÇÒÁö °áÁ¤ÇÑ´Ù.
¡à Protein structure
polypeptide°¡ synthesizeµÇ¸é chainÀÌ ÀÚ¿¬½º·´°Ô foldµÇ¾î ±× proteinÀÇ functional confromationÀ» ÀÌ·é´Ù.
¡æ proteinÀÇ structure´Â chainÀÇ °¢ ºÎºÐ»çÀÌÀÇ ´Ù¾çÇÑ chemical bonds¿¡ ÀÇÇØ À¯ÁöµÈ´Ù.
¨ç Primary structure (ÀÏÂ÷±¸Á¶)
- amino acidsÀÇ unigue sequence (peptide bond·Î¸¸ Çü¼ºµÈ »óÅÂÀÇ ±¸Á¶)
- proteinÀÇ precise primary structure´Â amino acidÀÇ random linkingÀÌ ¾Æ´Ñ genetic informationÀÇ inheritance¿¡ ÀÇÇØ °áÁ¤µÈ´Ù.
- sickle-cell disease ¡æ one point mutation ; amino acid Çϳª¸¸ ¹Ù²î¸é ÀüüÀÇ hemoglobinÀÇ ±¸Á¶°¡ ¹Ù²î¾î sickle-cellÀÇ ¸ð¾çÀ» ³ªÅ¸³ª°Ô µÇ¾î Á¤»óÀûÀÎ hemoglobin ±â´ÉÀ» ¸øÇÏ°Ô µÈ´Ù.
¨è Secondary structure (ÀÌÂ÷±¸Á¶)
´ëºÎºÐÀÇ proteinÀº proteinÀÇ overall conformation¿¡ ±â¿©ÇÏ´Â pattern¿¡¼ ¹Ýº¹ÀûÀ¸·Î coiledµÇ°Å³ª foldedµÈ polypeptideÀÇ segment¸¦ °¡Áø´Ù.
¡æ ÀÌ coils¿Í folds¸¦ secondary structure¶ó°í ÇÑ´Ù.
backboneÀÇ weak negative chargeÀÎ nitrogen, oxygen atomÀε¥, nitrogen atom¿¡ ºÙ¾îÀÖ´Â weakly hydrogen atomÀÌ peptide bond ±ÙóÀÇ oxygen atom¿¡ affinity¸¦ °¡Áö¹Ç·Î polypeptide backboneÀ» µû¶ó ÀÏÁ¤ÇÑ intervalsÀÇ hydrogen bond¸¦ Çü¼ºÇÏ°Ô µÈ´Ù.
- ¥á helix : 4°³ÀÇ peptide bond¸¶´Ù hydrogen bonding¿¡ ÀÇÇØ ÇÔ²² coiledµÊ (n¹ø° amino acid¿Í N+1¹ø° amino acid »çÀÌ¿¡ Çü¼ºµÈ´Ù.)
- ¥â sheet ( = pleated sheet) : polypeptide chainÀÇ ¾Õ µÚ·Î Á¢Èù ¸ð½À. chainÀÇ µÎ regionÀÌ ¼·Î ÆòÇàÇÏ´Ù. ±× »çÀÌ¿¡ ¸¹Àº hydrogen bonds°¡ Çü¼ºµÈ´Ù. ¡æ ¸¹Àº globular proteinÀÇ dense core¸¦ ¸¸µë
¨é Tertiary structure
- secondary structureÀÇ superimposedÇÑ pattern
- ´Ù¾çÇÑ amino acidÀÇ side chain »çÀÌÀÇ bonding¿¡¼ irregular contortions·Î ±¸¼ºµÊ. ¡æ hydrophobic attraction¿¡ ÀÇÇØ ±¸Á¶°¡ Çü¼ºµÈ´Ù.
- hydrophobic side chain : ¹°°úÀÇ mutual exclusionÀº hydrophobic side chains¸¦ localized clusters·Î À¯ÁöÇÏ°Ô ÇÏ°í proteinÀÇ core¿¡ ¸ðÀÌ°Ô ÇÔ
- hydrogen bond°¡ hydrophilic molecule°ú water »çÀÌ¿¡¼¿Í ¾î¶² amino acids »çÀÌ¿¡¼ Çü¼ºÀÌ µÈ´Ù.
- inonic bond°¡ charged side chains »çÀÌ¿¡¼ »ý¼ºµÈ´Ù.
¡Å cumulative effect°¡ proteinÀÌ specific shape¸¦ °®µµ·Ï µµ¿ÍÁØ´Ù.
- disulfide bond : strong covalent bond (--- SH HS ---), µÎ cysteine monomers¿¡¼ Çü¼ºµÇ´Â disulfide bridge
¡æ protein folding¿¡¼ ´õ¿í °¡±õ°Ô Á¢±ÙÇϵµ·Ï ±×¸®°í ´Ü´ÜÇÏ°Ô °íÁ¤½ÃÅ°´Â ¿ªÇÒÀ» ÇÔ.
¡Å proteinÀÇ 3Â÷¿ø ±¸Á¶¸¦ ÁöÅÊÇÏ´Â ¿ä¼Ò : hydrogen bond, disulfide bond, ionic bond, hydrophobic attraction, Van der waals force
¨ê Qeaternery structure
µÎ °³ ÀÌ»óÀÇ µ¶¸³µÈ polypeptide chains°¡ ¸ð¿© ÇϳªÀÇ functional macromoleculeÀ» Çü¼ºÇÑ´Ù. ¡æ polypeptide subunitsÀÇ aggregationÀÇ °á°úÀÎ overall protein structure
¡à Protein conformationÀÇ ¿ä°Ç
protein's enviromentÀÇ physical and conditions (pH, salt consentration, temperature)¿¡ ÀÇÁ¸ÇÑ´Ù.
- denaturation : proteinÀÌ unravel µÇ°í ±×°ÍÀÇ native conformationÀ» ÀÒ´Â °Í. denatured protein = biological inactive
- chaperone proteins : ´Ù¸¥ proteinsÀÇ foldingÀ» assistÇÏ´Â temporary braces °°Àº functional molecule
¡à Nucleic Acids
- central dogma
ÇÙ¾ÈÀÇ chromosome¿¡ ÀÖ´Â DNA sequence¿¡¼ geneÀÌ RNA polymerase¿¡ ÀÇÇØ transcriptionµÇ¾î RNA°¡ ¸¸µé¾îÁö°í ±× Áß mRNA°¡ ÇÙÀÇ pore¸¦ ÅëÇØ cytoplasmÀ¸·Î ³ª¿Í¼ libosome°ú °áÇÕÇÏ¿© mRNA sequenceÀÇ sense codon°ú amino acid¸¦ °¡Áö°í ÀÖ´Â t-RNA anti sense codonÀÇ °áÇÕÀ» libosomeÀÇ Áß°³·Î amin acidsÀÇ chainÀÎ polypeptide¸¦ Çü¼ºÇÏ°Ô µÇ´Â °ÍÀ» ÀǹÌÇÑ´Ù.
- nucleic acids : polymer DNA¸¦ ±¸¼ºÇÏ´Â monomer
- nucleotide : nucleic acids ±¸¼ºÇÏ´Â monomer
- DNA double strand : DNA´Â A-T base³¢¸® G-C base³¢¸® hydrogen bond¸¦ ÀÌ·ç¸é¼ helix ±¸Á¶¸¦ °¡Áø double stranded DNAÀÇ ±¸Á¶¸¦ °¡Áø´Ù.
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