1. AP Biology Mrs. Ramon

2. The Molecules of Life Macromolecules LARGE molecules Four classes: 1. Carbohydrates 2. Lipids (Fats) 3. Proteins 4. Nucleic Acids How are macromolecules made? Activity: Making and Breaking Polymers

3. Carbohydrates Functions Fuel Binding material Monomer Monosaccharides (CH 2 O) Polymer Polysaccharides Bond Glycosidic linkage Activity: Carbohydrates

4. Fig. 5-3 Dihydroxyacetone Ribulose Ketoses Aldoses Fructose Glyceraldehyde Ribose Glucose Galactose Hexoses (C 6 H 12 O 6 ) Pentoses (C 5 H 10 O 5 ) Trioses (C 3 H 6 O 3 )

5. Fig. 5-6 (b) Glycogen: an animal polysaccharide Starch Glycogen Amylose Chloroplast (a) Starch: a plant polysaccharide Amylopectin Mitochondria Glycogen granules 0.5 µm 1 µm

6. Fig. 5-9

7. Fig. 5-10 The structure of the chitin monomer. (a) (b) (c) Chitin forms the exoskeleton of arthropods. Chitin is used to make a strong and flexible surgical thread.

8. Lipids Components Glycerol and fatty acids Bond Ester linkage Three types: 1. Fats 2. Phospholipids 3. Steroids

9. Fig. 5-11 Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol)

10. 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

11. Fig. 5-13 (b) Space-filling model (a)(c) Structural formula Phospholipid symbol Fatty acids Hydrophilic head Hydrophobic tails Choline Phosphate Glycerol Hydrophobic tails Hydrophilic head

12. Fig. 5-14 Hydrophilic head Hydrophobic tail WATER

13. Fig. 5-15

14. Proteins Functions Structure Storage Transport Hormones Signaling Movement Defense Enzymatic Monomer Amino acid Polymer Polypeptide Bond Peptide bond

15. Fig. 5-16 Enzyme (sucrase) Substrate (sucrose) Fructose Glucose OH H O H2OH2O

16. Fig. 5-UN1 Amino group Carboxyl group  carbon

17. Fig. 5-17a Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I ) Methionine (Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P)

18. Fig. 5-17b Polar Asparagine (Asn or N) Glutamine (Gln or Q) Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y)

19. Fig. 5-17c Acidic Arginine (Arg or R) Histidine (His or H) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Basic Electrically charged

20. Fig. 5-19 A ribbon model of lysozyme (a)(b) A space-filling model of lysozyme Groove

21. Fig. 5-20 Antibody protein Protein from flu virus

22. Fig. 5-21 Primary Structure Secondary Structure Tertiary Structure  pleated sheet Examples of amino acid subunits + H 3 N Amino end  helix Quaternary Structure

23. Fig. 5-21f Polypeptide backbone Hydrophobic interactions and van der Waals interactions Disulfide bridge Ionic bond Hydrogen bond

24. Fig. 5-21g Polypeptide chain  Chains Heme Iron  Chains Collagen Hemoglobin

25. Fig. 5-22 Primary structure Secondary and tertiary structures Quaternary structure Normal hemoglobin (top view) Primary structure Secondary and tertiary structures Quaternary structure Function  subunit Molecules do not associate with one another; each carries oxygen. Red blood cell shape Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. 10 µm Normal hemoglobin     1234567 Val His Leu ThrPro Glu Red blood cell shape  subunit Exposed hydrophobic region Sickle-cell hemoglobin   Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced.   Fibers of abnormal hemoglobin deform red blood cell into sickle shape. 10 µm Sickle-cell hemoglobin GluPro Thr Leu His Val 1234567

26. Fig. 5-22c Normal red blood cells are full of individual hemoglobin molecules, each carrying oxygen. Fibers of abnormal hemoglobin deform red blood cell into sickle shape. 10 µm

27. Fig. 5-23 Normal protein Denatured protein Denaturation Renaturation

28. Nucleic Acids Functions Genetic info. Monomer Nucleotide Polymer Polynucleotides Bond Phosphodiester linkage

29. Fig. 5-26-3 mRNA Synthesis of mRNA in the nucleus DNA NUCLEUS mRNA CYTOPLASM Movement of mRNA into cytoplasm via nuclear pore Ribosome Amino acids Polypeptide Synthesis of protein 1 2 3

30. Fig. 5-27 5 end Nucleoside Nitrogenous base Phosphate group Sugar (pentose) (b) Nucleotide (a) Polynucleotide, or nucleic acid 3 end 3C3C 3C3C 5C5C 5C5C Nitrogenous bases Pyrimidines Cytosine (C) Thymine (T, in DNA)Uracil (U, in RNA) Purines Adenine (A)Guanine (G) Sugars Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars

31. Fig. 5-28 Sugar-phosphate backbones 3' end 5' end Base pair (joined by hydrogen bonding) Old strands New strands Nucleotide about to be added to a new strand

32. Fig. 5-UN9

33. You should now be able to: 1. List and describe the four major classes of molecules 2. Describe the formation of a glycosidic linkage and distinguish between monosaccharides, disaccharides, and polysaccharides 3. Distinguish between saturated and unsaturated fats 4. Describe the four levels of protein structure 5. 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