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Download Chapter 5: Structure and Function of Macromolecules
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AP Biology Mrs. Ramon The Molecules of Life Macromolecules LARGE molecules Four classes: Carbohydrates 2. Lipids (Fats) 3. Proteins 4. Nucleic Acids 1. How are macromolecules made? Activity: Making and Breaking Polymers Carbohydrates Functions Fuel Binding material Monomer Monosaccharides (CH2O) Polymer Polysaccharides Bond Glycosidic linkage Activity: Carbohydrates Fig. 5-3 Trioses (C3H6O3) Pentoses (C5H10O5) Hexoses (C6H12O6) Glyceraldehyde Ribose Glucose Galactose Dihydroxyacetone Ribulose Fructose Fig. 5-6 Chloroplast Mitochondria Glycogen granules Starch 0.5 µm 1 µm Glycogen Amylose Amylopectin (a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide Fig. 5-9 Fig. 5-10 (a) The structure of the chitin monomer. (b) Chitin forms the exoskeleton of arthropods. (c) Chitin is used to make a strong and flexible surgical thread. Lipids Components Glycerol and fatty acids Bond Ester linkage Three types: 1. Fats 2. Phospholipids 3. Steroids Fig. 5-11 Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol) Fig. 5-12 Structural formula of a saturated fat molecule Stearic acid, a saturated fatty acid (a) Saturated fat Structural formula of an unsaturated fat molecule Oleic acid, an unsaturated fatty acid (b) Unsaturated fat cis double bond causes bending Hydrophobic tails Hydrophilic head Fig. 5-13 (a) Structural formula Choline Phosphate Glycerol Fatty acids Hydrophilic head Hydrophobic tails (b) Space-filling model (c) Phospholipid symbol Fig. 5-14 Hydrophilic head Hydrophobic tail WATER WATER Fig. 5-15 Proteins Functions Structure Storage Transport Hormones Signaling Movement Defense Enzymatic Monomer Amino acid Polymer Polypeptide Bond Peptide bond Fig. 5-16 Substrate (sucrose) Glucose Enzyme (sucrase) OH Fructose HO H2O Fig. 5-UN1 carbon Amino group Carboxyl group Fig. 5-17a Nonpolar Glycine (Gly or G) Methionine (Met or M) Alanine (Ala or A) Valine (Val or V) Phenylalanine (Phe or F) Leucine (Leu or L) Tryptophan (Trp or W) Isoleucine (Ile or I) Proline (Pro or P) Fig. 5-17b Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine Glutamine (Asn or N) (Gln or Q) Fig. 5-17c Electrically charged Acidic Aspartic acid Glutamic acid (Glu or E) (Asp or D) Basic Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H) Fig. 5-19 Groove Groove (a) A ribbon model of lysozyme (b) A space-filling model of lysozyme Fig. 5-20 Antibody protein Protein from flu virus Fig. 5-21 Primary Structure Secondary Structure pleated sheet +H N 3 Amino end Examples of amino acid subunits helix Tertiary Structure Quaternary Structure Fig. 5-21f Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond Fig. 5-21g Polypeptide chain Chains Iron Heme Chains Hemoglobin Collagen Fig. 5-22 Normal hemoglobin Primary structure Val His Leu Thr Pro Glu Glu 1 2 3 4 5 6 7 Secondary and tertiary structures subunit Function Normal hemoglobin (top view) Secondary and tertiary structures 1 2 3 Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. 6 7 subunit Sickle-cell hemoglobin Function Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. 10 µm Red blood cell shape 5 Exposed hydrophobic region Molecules do not associate with one another; each carries oxygen. 4 Quaternary structure Val His Leu Thr Pro Val Glu Quaternary structure Sickle-cell hemoglobin Primary structure 10 µm Red blood cell shape Fibers of abnormal hemoglobin deform red blood cell into sickle shape. Fig. 5-22c 10 µm Normal red blood cells are full of individual hemoglobin molecules, each carrying oxygen. 10 µm Fibers of abnormal hemoglobin deform red blood cell into sickle shape. Fig. 5-23 Denaturation Normal protein Renaturation Denatured protein Nucleic Acids Functions Genetic info. Monomer Nucleotide Polymer Polynucleotides Bond Phosphodiester linkage Fig. 5-26-3 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore Ribosome 3 Synthesis of protein Polypeptide Amino acids Fig. 5-27 5 end Nitrogenous bases Pyrimidines 5C 3C Nucleoside Nitrogenous base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Phosphate group 5C Sugar (pentose) Adenine (A) Guanine (G) (b) Nucleotide 3C Sugars 3 end (a) Polynucleotide, or nucleic acid Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars Fig. 5-28 5' end 3' end Sugar-phosphate backbones Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 3' end 5' end New strands 5' end 3' end 5' end 3' end Fig. 5-UN9 You should now be able to: 1. 2. 3. 4. 5. List and describe the four major classes of molecules Describe the formation of a glycosidic linkage and distinguish between monosaccharides, disaccharides, and polysaccharides Distinguish between saturated and unsaturated fats Describe the four levels of protein structure Distinguish between the following pairs: pyrimidine and purine, nucleotide and nucleoside, ribose and deoxyribose, the 5 end and 3 end of a nucleotide Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
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