1. Unit 2: Pre-test –Avg = 5 (out of 23) –Range = unknown Termites –Follow Paper Mate ink –Acts as a pheromone Test corrections – due tomorrow I will scream sometime during class today.

2. The Structure and Function of Macromolecules Chapter 5

3. 1.What are the 4 major macromolecules? –Carbohydrates –Proteins –Lipids –Nucleic acids 2.How are they all similar? –All large polymers made of smaller monomers –All formed the same way Chapter 5 The Structure and Function of Macromolecules

4. (a) Dehydration reaction in the synthesis of a polymer HOH 1 2 3 H 1 23 4 H H2OH2O Short polymer Unlinked monomer Longer polymer Dehydration removes a water molecule, forming a new bond Figure 5.2A (b) Hydrolysis in the breaking down of a polymer HO 1 2 3 H H 1 2 3 4 H2OH2O H Hydrolysis adds a water molecule, breaking a bond Figure 5.2B Figure 5.2 The synthesis and breakdown of polymers

5. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? –Sugars –Made of monosaccharides CH 2 0 Sugars end in -ose Nutrient for cells (1° glucose) Carbon skeleton is used for other organic molecules Chapter 5 The Structure and Function of Macromolecules

6. Triose sugars (C 3 H 6 O 3 ) Pentose sugars (C 5 H 10 O 5 ) Hexose sugars (C 6 H 12 O 6 ) H C OH HO C H H C OH HO C H H C OH C O H C OH HO C H H C OH C O H H H HHH H H HHH H H H C CCC O O O O Aldoses Glyceraldehyde Ribose Glucose Galactose Dihydroxyacetone Ribulose Ketoses Fructose Figure 5.3 Figure 5.3 Examples of monosaccharides

7. Figure 5.4 Linear & ring forms of glucose H H C OH HO C H H C OH H C O C H 1 2 3 4 5 6 H OH 4C4C 6 CH 2 OH 5C5C H OH C H OH H 2 C 1C1C H O H OH 4C4C 5C5C 3 C H H OH OH H 2C2C 1 C OH H CH 2 OH H H OH HO H OH H 5 3 2 4 (a) Linear and ring forms. Chemical equilibrium between the linear and ring structures greatly favors the formation of rings. To form the glucose ring, carbon 1 bonds to the oxygen attached to carbon 5. OH 3 O H O O 6 1 Figure 5.4

8. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? 4.How are monomers added to carbs? Chapter 5 The Structure and Function of Macromolecules Dehydration reaction in the synthesis of maltose. The bonding of two glucose units forms maltose. The glycosidic link joins the number 1 carbon of one glucose to the number 4 carbon of the second glucose. Joining the glucose monomers in a different way would result in a different disaccharide. Dehydration reaction in the synthesis of sucrose. Sucrose is a disaccharide formed from glucose and fructose. Notice that fructose, though a hexose like glucose, forms a five-sided ring. (a) (b) H HO H H OH H OH O H CH 2 OH H HO H H OH H OH O H CH 2 OH H O H H OH H OH O H CH 2 OH H H2OH2O H2OH2O H H O H HO H OH O H CH 2 OH HO OH H CH 2 OH H OH H H HO OH H CH 2 OH H OH H O O H OH H CH 2 OH H OH H O H OH CH 2 OH H HO O CH 2 OH H H OH O O 1 2 1 4 1– 4 glycosidic linkage 1–2 glycosidic linkage Glucose Fructose Maltose Sucrose OH H H

9. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? 4.How are monomers added to carbs? 5.What are polysaccharides used for? –Energy storage Starch – plants Glycogen – animals –Structural support Cellulose Chitin Chapter 5 The Structure and Function of Macromolecules

10. Mitochondria Giycogen granulesChloroplast Starch Amylose Amylopectin 1  m 0.5  m (a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide Glycogen

11. H O O CH 2 O H H OH H H H H HO 4 C C C C C C H H H OH H H O CH 2 O H H H H OH H H HO 4 OH CH 2 O H O OH HO 4 1 O CH 2 O H O OH O CH 2 O H O OH CH 2 O H O OH O O CH 2 O H O OH HO 4 O 1 OH O O CH 2 O H O OH O O (a)  and  glucose ring structures (b) Starch: 1– 4 linkage of  glucose monomers 1  glucose  glucose CH 2 O H 1 4 4 1 1 (c) Cellulose: 1– 4 linkage of  glucose monomers 6. Why do we poop corn?

12. Chapter 5 The Structure and Function of Macromolecules Cellulose molecules Plant cells 0.5  m Cell walls Cellulose microfibrils in a plant cell wall  Microfibril CH 2 OH OH O O O CH 2 OH O O OH O CH 2 OH OH O O CH 2 OH O O OH CH 2 OH O O OH O O CH 2 OHOH CH 2 OHOH O O CH 2 OH OH O CH 2 OH O O OHCH 2 OH OH  Glucose monomer O O O O O O Parallel cellulose molecules are held together by hydrogen bonds between hydroxyl groups attached to carbon atoms 3 and 6. About 80 cellulose molecules associate to form a microfibril, the main architectural unit of the plant cell wall. A cellulose molecule is an unbranched  glucose polymer. OH O O Figure 5.8 Cellulose

13. (a) The structure of the chitin monomer. O CH 2 OH OH H H H NH C CH 3 O H H (b) Chitin forms the exoskeleton of arthropods. This cicada is molting, shedding its old exoskeleton and emerging in adult form. (c) Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals. OH Chapter 5 The Structure and Function of Macromolecules

14. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? 4.How are monomers added to carbs? 5.What are polysaccharides used for? 6.Why do we poop corn? 7.What are some common lipids? –Fats –Phospholipids –Steroids –Oils –Waxes Chapter 5 The Structure and Function of Macromolecules

15. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? 4.How are monomers added to carbs? 5.What are polysaccharides used for? 6.Why do we poop corn? 7.What are some common lipids? 8.How are fats made? Chapter 5 The Structure and Function of Macromolecules

16. Figure 5.11 The synthesis and structure of a fat, or triacylglycerol

17. 1.What are the 4 major macromolecules? 2.How are they all similar? 3.What are carbohydrates & what are they made of? 4.How are monomers added to carbs? 5.What are polysaccharides used for? 6.Why do we poop corn? 7.What are some common lipids? 8.How are fats made? 9.What is the difference between a saturated & unsaturated fat? Chapter 5 The Structure and Function of Macromolecules

18. (a) Saturated fat and fatty acid Stearic acid (b) Unsaturated fat and fatty acid cis double bond causes bending Oleic acid Figure 5.12 Examples of saturated and unsaturated fats and fatty acids

19. Staple test corrections to test & place in box

20. Saturated vs Unsaturated Fats -No double bonds (C-C)- Double bonds (C=C) -Carbons are saturated - Carbons not saturated -Solid at RT- Oil at RT -Animal fats- Plant or fish fats -Butter- Vegetable oil -Bacon grease- Olive oil What are trans fats? -Formed by hydrogenation -C=C without the “kink”

21. Saturated vs Unsaturated Fats -No double bonds (C-C)- Double bonds (C=C) -Carbons are saturated - Carbons not saturated -Solid at RT- Oil at RT -Animal fats- Plant or fish fats -Butter- Vegetable oil -Bacon grease- Olive oil What are the functions of fats? -Energy storage (2X carbs) -Cushion -Insulation

22. Hydrophilic head CH 2 N(CH 3 ) 3 CH 2 O P O O O CH CH 2 OO C O C O Choline Phosphate Glycerol (a) Structural formula (b) Space-filling model Fatty acids (c) Phospholipid symbol Hydrophobic tails Hydrophilic head Hydrophobic tails + – Figure 5.13 The structure of a phospholipid Amphipathic – molecules both polar & non-polar

23. Hydrophilic head WATER Hydrophobic tail Figure 5.14 Bilayer structure formed by self-assembly of phospholipids in an aqueous environment

24. HO CH 3 H3CH3C Figure 5.15 Cholesterol, a steroid

25. 10. What are the monomers of proteins? -Amino acids 11.How are all amino acids similar? Chapter 5 The Structure and Function of Macromolecules H H N C R H C O OH Amino group Carboxyl group  carbon

26. S O O–O– O O–O– H H3N+H3N+ C C O O–O– H CH 3 H3N+H3N+ C H C O O–O– C C O O–O– H H3N+H3N+ CH CH 3 CH 2 C H H3N+H3N+ CH 3 CH 2 CH C H H3N+H3N+ C CH 3 CH 2 C H3N+H3N+ H C O O–O– C H3N+H3N+ H C O O–O– NH H C O O–O– H3N+H3N+ C CH 2 H2CH2C H2NH2N C H C Nonpolar Glycine (Gly) Alanine (Ala) Valine (Val)Leucine (Leu)Isoleucine (Ile) Methionine (Met) Phenylalanine (Phe) C O O–O– Tryptophan (Trp) Proline (Pro) H3CH3C Figure 5.17 The 20 amino acids of proteins

28. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? -Dehydration (condensation) rxn -Creates a peptide bond Chapter 5 The Structure and Function of Macromolecules

29. Carboxyl end (C-terminus) DESMOSOMES OH DESMOSOMES OH CH 2 C N H C H O HOH Peptide bond OH H H HH H H H H H H H H N N N N N SH Side chains SH OO OO O H2OH2O CH 2 C C C CCC C C C C Peptide bond Amino end (N-terminus) Backbone (a) (b) Figure 5.18 Making a polypeptide chain

30. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? 13.What are the 4 levels of protein structure? -1° (Primary) – aa sequence (determined by DNA sequence) -2° (Secondary) – based on H-bonds -3° (Tertiary) – overall globular shape – 3D structure -4° (Quaternary) – several 3° polypeptides (subunits) Chapter 5 The Structure and Function of Macromolecules

31. Figure 5.20 Primary structure of a protein Based on amino acid sequence Each protein has a unique sequence Like the alphabet (letters = aa) – Amino acid subunits + H 3 N Amino end o Carboxyl end o c Gly ProThr Gly Thr Gly Glu Seu Lys Cys Pro Leu Met Val Lys Val Leu Asp Ala Val Arg Gly Ser Pro Ala Gly lle Ser Pro Phe His Glu His Ala Glu Val Phe Thr Ala Asn Asp Ser Gly Pro Arg Tyr Thr lle Ala Leu Ser Pro Tyr Ser Tyr Ser Thr Ala Val Thr Asn Pro Lys Glu Thr Lys Ser Tyr Trp Lys Ala Leu Glu Lle Asp

32. OC  helix  pleated sheet Amino acid subunits N C H C O C N H C O H R C N H C O H C R N H H R C O R C H N H C O H N C O R C H N H H C R C O H C R N H C O C C O C N H H R C C O N H H C R C O N H R C H C O N H H C R C O N H R C H C O N H H C R C O N H R C H C O N H C N H H C R N H O O C N C R C H H O C H R N H O C R C H N H O C H C R N H C C N R H H O C H C R N H O C R C H Figure 5.20 Secondary structure of a protein Based on H-bonds α-helix- β-pleated sheet adjacent polar aa - after folding, polar aa become neighbors and form H-bonds

33. Figure 5.20 Tertiary structure CH 2 OHOH O C OH CH 2 NH 3 + C -O-O CH 2 O SS CH CH 3 H3CH3C H3CH3C Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Ionic bond Disulfide bridge overall globular shape – 3D structure each protein has unique 3D shape recall carbon sets the 3D shape based on 1° structure (aa sequence) rearranged the alphabet to get new words Disulfide bridge 2 cysteine amino acids covalent bond van der Waals interactions hydrophobic interactions ionic bonds occasional H-bonds

34. Figure 5.20 Quarternary structure Polypeptide chain Collagen  Chains  Chains Hemoglobin Iron Heme more than one 3° polypeptide (subunit) needed for biological activity not all proteins have quarternary structure # of subunits varies by protein

35. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? 13.What are the 4 levels of protein structure? 14.How much does sequence (structure) influence function? -Sickle cell anemia Chapter 5 The Structure and Function of Macromolecules

36. Primary structure Secondary and tertiary structures Quaternary structure Function Red blood cell shape Hemoglobin A Molecules do not associate with one another; each carries oxygen Normal cells are full of individual hemoglobin molecules, each carrying oxygen     10  m     Primary structure Secondary and tertiary structures Quaternary structure Function Red blood cell shape Hemoglobin S Molecules interact with one another to crystallize into a fiber, capacity to carry oxygen is greatly reduced Fibers of abnormal hemoglobin deform cell into sickle shape  subunit 1234 56734 567 21 Normal hemoglobin Sickle-cell hemoglobin... Val His Leu Thr Pro Glu Glu Val His Leu Thr Pro Val Glu Figure 5.21 A single amino acid substitution in a protein causes sickle-cell disease

37. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? 13.What are the 4 levels of protein structure? 14.How much does sequence (structure) influence function? 15.What happens to proteins if they get too hot or experience a change in pH? Chapter 5 The Structure and Function of Macromolecules Denaturation Renaturation Denatured protein Normal protein

38. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? 13.What are the 4 levels of protein structure? 14.How much does sequence (structure) influence function? 15.What happens to proteins if they get too hot or experience a change in pH? 16.What do proteins do? Chapter 5 The Structure and Function of Macromolecules

39. Table 5.1 Protein function ↓

40. 10. What are the monomers of proteins? 11.How are all amino acids similar? 12.How are amino acids connected? 13.What are the 4 levels of protein structure? 14.How much does sequence (structure) influence function? 15.What happens to proteins if they get too hot or experience a change in pH? 16.What do proteins do? 17.What are the different types of nucleic acids? -DNA – deoxyribonucleic acid -RNA – ribonucleic acid -mRNA – messenger -tRNA – transfer -rRNA – ribosomal 18.What are the monomers of nucleic acids? 19.What makes up the monomers? Chapter 5 The Structure and Function of Macromolecules

41. 3’C CH Uracil (in RNA) U 5’ end 5’C 3’C 5’C O O O O 3’ end OH Nitrogenous base Nucleoside O O OO OO P CH 2 O 5’C 3’C Phosphate group Pentose sugar (b) Nucleotide C N N C O H NH 2 CH O C N H HN C O C CH 3 N HN C C H O O Cytosine C Thymine (in DNA) T N HC N C C N C CH N NH 2 O N HC N H H C C C N NH C NH 2 Adenine A Guanine G Purines O HOCH 2 H H H OH H O HOCH 2 H H H OH H H 5’ 4 3’ 2’ 1’ 3’ 2’ 1’ 4 5’ Pentose sugars Deoxyribose (in DNA) Ribose (in RNA) Nitrogenous bases Pyrimidines (c) Nucleoside components (a) Polynucleotide, or nucleic acid Figure5.26 Components of nucleic acids

42. 3 end Sugar-phosphate backbone Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand A 3 end 5 end New strands 3 end 5 end C G C G A T CG AT A T G C AT AT T A G A C C C G G T A A T C G A T G C A T A T T A C G A T A T G C T A A T T A C G A T T A C G T A C G G C T C G Figure 5.27 DNA Double helix