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Chapter 5. Macromolecules

Chapter 5. Macromolecules. Macromolecules. Smaller organic molecules join together to form larger molecules macromolecules 4 major classes of macromolecules: carbohydrates lipids proteins nucleic acids. Polymers. Long molecules built by linking chain of repeating smaller units

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Chapter 5. Macromolecules

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  1. Chapter 5. Macromolecules

  2. Macromolecules • Smaller organic molecules join together to form larger molecules • macromolecules • 4 major classes of macromolecules: • carbohydrates • lipids • proteins • nucleic acids

  3. Polymers • Long molecules built by linking chain of repeating smaller units • polymers • monomers = repeated small units • covalent bonds

  4. How to build a polymer • Condensation reaction • dehydration synthesis • joins monomers by “taking” H2O out • 1 monomer provides OH • the other monomer provides H • together these form H2O • requires energy & enzymes

  5. How to break down a polymer • Hydrolysis • use H2O to break apart monomers • reverse of condensation reaction • H2O is split into H and OH • H & OH group attach where the covalent bond used to be • ex: digestion is hydrolysis

  6. Carbohydrates

  7. Carbohydrates • Carbohydrates are composed of C, H, O carbo - hydr - ate CH2O (CH2O)x C6H12O6 • Function: • energy u energy storage • raw materials u structural materials • Monomer: sugars • ex: sugars & starches

  8. Sugars • Most names for sugars end in -ose • Classified by number of carbons • 6C = hexose (glucose) • 5C = pentose (fructose, ribose) • 3C = triose (glyceraldehyde)

  9. Simple & complex sugars • Monosaccharides • simple 1 monomer sugars • glucose • Disaccharides • 2 monomers • sucrose • Polysaccharides • large polymers • starch

  10. Building sugars • Dehydration synthesis monosaccharides disaccharide | glucose | glucose | maltose glycosidic linkage

  11. Polysaccharides • Polymers of sugars • costs little energy to build • easily reversible = release energy • Function: • energy storage • starch (plants) • glycogen (animals) • building materials = structure • cellulose (plants) • chitin (arthropods & fungi)

  12. Polysaccharide diversity • Molecular structure determines function • isomers of glucose • How does structure influence function…

  13. Digesting starch vs. cellulose

  14. Cow can digest cellulose well; no need to eat supplemental sugars Gorilla can’t digest cellulose well; must supplement with sugar source, like fruit

  15. Glycemic index • Which food will get into your blood more quickly? • apple • rice cakes • corn flakes • bagel • peanut M&M

  16. Glycemic index • Which food will get into your blood more quickly? • apple 36 • rice cakes 82 • corn flakes 84 • bagel 72 • peanut M&M 33

  17. Lipids

  18. Lipids • Lipids are composed of C, H, O • long hydrocarbon chain • Diverse group • fats • phospholipids • steroids • Do not form polymers • big molecules made of subunit smaller molecules • not a continuing chain

  19. Fats • Structure: • glycerol (3C alcohol) + fatty acid • fatty acid = long HC “tail” with COOH group at “head” dehydration synthesis

  20. Fat • Triacylglycerol • 3 fatty acids linked to glycerol • ester linkage = between OH & COOH

  21. Dehydration synthesis

  22. Fats • Long HC chain • polar or non-polar? • hydrophilic or hydrophobic? • Function: • energy storage • very rich • 2x carbohydrates • cushion organs • insulates body • think whale blubber! “Let’s go to the video tape!” (play movie here)

  23. Saturated fats • All C bonded to H • No C=C double bonds • long, straight chain • most animal fats • solid at room temp. • contributes to cardiovascular disease (atherosclerosis) = plaque deposits

  24. Unsaturated fats • C=C double bonds in the fatty acids • plant & fish fats • vegetable oils • liquid at room temperature • the kinks made by double bonded C prevent the molecules from packing tightlytogether

  25. Cholesterol • Important cell component • animal cell membranes • precursor of all other steroids • including vertebrate sex hormones • high levels in blood may contribute to cardiovascular disease

  26. Proteins

  27. Proteins • Most structurally & functionally diverse group of biomolecules • Function: • involved in almost everything • enzymes • structure (keratin, collagen) • carriers & transport (membrane channels) • receptors & binding (defense) • contraction (actin & myosin) • signaling (hormones) • storage (bean seed proteins)

  28. Proteins • Structure: • monomer = amino acids • 20 different amino acids • polymer = polypeptide • protein can be 1 or more polypeptide chains folded & bonded together • large & complex molecules • complex 3-D shape

  29. Structure: • central carbon • amino group • carboxyl group (acid) • R group (side chain) • variable group • confers unique chemical properties of the amino acid O H | —C— | H || C—OH —N— H R Amino acids

  30. nonpolar & hydrophobic Why are these nonpolar & hydrophobic? Nonpolar amino acids

  31. polar or charged & hydrophilic Why are these polar & hydrophillic? Polar amino acids

  32. Building proteins • Peptide bonds: dehydration synthesis • linking NH2 of 1 amino acid to COOH of another • C–N bond peptidebond

  33. Building proteins • Polypeptide chains • N-terminal = NH2 end • C-terminal = COOH end • repeated sequence (N-C-C) is the polypeptide backbone • grow in one direction

  34. hemoglobin collagen Protein structure & function • function depends on structure • 3-D structure • twisted, folded, coiled into unique shape pepsin

  35. lysozyme: enzyme in tears & mucus that kills bacteria the 10 glycolytic enzymes used to breakdown glucose to make ATP “Let’s go to the video tape!” (play movie here) Protein structure & function • function depends on structure • all starts with the order of amino acids • what determines that order of amino acids?

  36. Primary (1°) structure • Order of amino acids in chain • amino acid sequence determined by DNA • slight change in amino acid sequence can affect protein’s structure & it’s function • even just one amino acid change can make all the difference!

  37. “Let’s go to the video tape!” (play movie here) Sickle cell anemia

  38. Denature a protein • Disrupt 3° structure • pH salt • temperature • unravel or denature protein • disrupts H bonds, ionic bonds & disulfide bridges • Some proteins can return to their functional shape after denaturation, many cannot

  39. Any Questions??

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