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AP Biology 2005-2006 Chapter 5. Macromolecules
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AP Biology 2005-2006 Macromolecules Smaller organic molecules join together to form larger molecules macromolecules 4 major classes of macromolecules: carbohydrates lipids proteins nucleic acids
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AP Biology 2005-2006 Polymers Long molecules built by linking chain of repeating smaller units polymers monomers = repeated small units covalent bonds
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AP Biology 2005-2006 How to build a polymer Condensation reaction dehydration synthesis joins monomers by “taking” H 2 O out 1 monomer provides OH the other monomer provides H together these form H 2 O requires energy & enzymes
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AP Biology 2005-2006 How to break down a polymer Hydrolysis use H 2 O to break apart monomers reverse of condensation reaction H 2 O is split into H and OH H & OH group attach where the covalent bond used to be ex: digestion is hydrolysis
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AP Biology 2005-2006 Carbohydrates
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AP Biology 2005-2006 Carbohydrates Carbohydrates are composed of C, H, O carbo - hydr - ate CH 2 O (CH 2 O) x C 6 H 12 O 6 Function: energy u energy storage raw materials u structural materials Monomer: sugars ex: sugars & starches
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AP Biology 2005-2006 Sugars Most names for sugars end in -ose Classified by number of carbons 6C = hexose (glucose) 5C = pentose (fructose, ribose) 3C = triose (glyceraldehyde)
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AP Biology 2005-2006 Simple & complex sugars Monosaccharides simple 1 monomer sugars glucose Disaccharides 2 monomers sucrose Polysaccharides large polymers starch
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AP Biology 2005-2006 Building sugars Dehydration synthesis | glucose | glucose glycosidic linkage monosaccharidesdisaccharide | maltose
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AP Biology 2005-2006 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)
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AP Biology 2005-2006 Polysaccharide diversity Molecular structure determines function isomers of glucose How does structure influence function…
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AP Biology 2005-2006 Digesting starch vs. cellulose
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AP Biology 2005-2006 Cow can digest cellulose well; no need to eat supplemental sugars Gorilla can’t digest cellulose well; must supplement with sugar source, like fruit
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AP Biology 2005-2006 Glycemic index Which food will get into your blood more quickly? apple rice cakes corn flakes bagel peanut M&M
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AP Biology 2005-2006 Glycemic index Which food will get into your blood more quickly? apple36 rice cakes82 corn flakes84 bagel72 peanut M&M33
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AP Biology 2005-2006 Lipids
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AP Biology 2005-2006 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
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AP Biology 2005-2006 Fats Structure: glycerol (3C alcohol) + fatty acid dehydration synthesis fatty acid = long HC “tail” with COOH group at “head”
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AP Biology 2005-2006 Fat Triacylglycerol 3 fatty acids linked to glycerol ester linkage = between OH & COOH
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AP Biology 2005-2006 Dehydration synthesis
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AP Biology 2005-2006 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)play movie here
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AP Biology 2005-2006 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
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AP Biology 2005-2006 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 tightly together
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AP Biology 2005-2006 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
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AP Biology 2005-2006 Proteins
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AP Biology 2005-2006 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)
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AP Biology 2005-2006 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
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AP Biology 2005-2006 Amino acids Structure: central carbon amino group carboxyl group (acid) R group (side chain) variable group confers unique chemical properties of the amino acid —N——N— H H H | —C— | C—OH || O R
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AP Biology 2005-2006 Nonpolar amino acids nonpolar & hydrophobic Why are these nonpolar & hydrophobic?
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AP Biology 2005-2006 Polar amino acids polar or charged & hydrophilic Why are these polar & hydrophillic?
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AP Biology 2005-2006 Building proteins Peptide bonds: dehydration synthesis linking NH 2 of 1 amino acid to COOH of another C–N bond peptide bond
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AP Biology 2005-2006 Building proteins Polypeptide chains N-terminal = NH 2 end C-terminal = COOH end repeated sequence (N-C-C) is the polypeptide backbone grow in one direction
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AP Biology 2005-2006 Protein structure & function hemoglobin function depends on structure 3-D structure twisted, folded, coiled into unique shape collagen pepsin
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AP Biology 2005-2006 Protein structure & function function depends on structure all starts with the order of amino acids what determines that order of amino acids? “Let’s go to the video tape!” (play movie here) lysozyme: enzyme in tears & mucus that kills bacteria the 10 glycolytic enzymes used to breakdown glucose to make ATP
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AP Biology 2005-2006 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!
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AP Biology 2005-2006 Sickle cell anemia “Let’s go to the video tape!” (play movie here)
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AP Biology 2005-2006 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
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AP Biology 2005-2006 Any Questions??
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