1. Happy Monday! 9/16/2013 PQ & Journal—7.5 & 7.6 Test Wednesday, let’s boogy!

2. D

3. 4 Macromolecules in all living organisms:

4. Table 3.1

5. Polymers are formed in condensation reactions.

6. Figure 3.4 Condensation of Polymers : Water is removed; Cov bond forms b/w monomers

7. Figure 3.4 Hydrolysis of Polymers– water is added; cov bond b/w monomers is broken

8. 6 Functions of proteins: (IB)

9. Proteins are made from 20 different amino acids (monomeric units)

10. The composition of a protein:

11. 7.5.2 Outline the difference between fibrous proteins & globular proteins, with reference to two examples of each protein type. FibrousGlobular Shape Solubility Main level of organization Function Examples

12. Parts of an amino acid Amino acids have

13. These hydrophylic amino acids attract ions of opposite charges. Table 3.2 (Part 1): HYDROPHILIC AMINO ACIDS

14. Hydrophylic amino acids with polar but uncharged side chains form hydrogen bonds Table 3.2 (Part 2): POLAR, UNCHARGED (HYDROPHILIC)

15. Table 3.2 (Part 3): NONPOLAR, HYDROPHOBIC Hydrophobic amino acids

16. Table 3.2 (Part 4): WEIRDOS

17. Figure 3.5 Disulfide Bridge FORMATION BETWEEN TWO CYSTEINES (covalent bond)

18. Figure 3.6 Formation of Peptide Bonds: amino of 1, carboxyl of another  peptide bond (condens.) The peptide bond is inflexible—no rotation is possible.

19. Primary Structure: Figure 3.7 The Four Levels of Protein Structure Amino acid monomersPeptide bond

20. Secondary structure: α helix— β pleated sheet—

21. Figure 3.7 The Four Levels of Protein Structure Secondary Structure:  Helix Hydrogen bond

22. Figure 3.7 The Four Levels of Protein Structure  Pleated sheet Secondary Structure: Hydrogen bond

23. Tertiary structure:

24. Figure 3.7 The Four Levels of Protein Structure Tertiary Structure  Pleated sheet  Helix Hydrogen bond Disulfide bridge

25. Quaternary structure results from the interaction of subunits by

26. Figure 3.7 The Four Levels of Protein Structure Quaternary Structure:

27. Figure 3.9 Quaternary Structure of a Protein

28. Figure 3.10 Noncovalent Interactions between Proteins and Other Molecules Ionic bonds b/w charged R groups 2 nonpolar groups interact hydrophobically H bonds form b/w 2 polar groups

29. Figure 3.11 Denaturation Is the Loss of Tertiary Protein Structure and Function Destroys its biological functions Renaturation: sometimes possible, but usually not

30. 6 Energy, Enzymes, and Metabolism Alcohol dehydrogenase: catalyst for breakdown of alcohol

31. Catalysts speed up the rate of a reaction.

32. Activation Energy

33. Enzyme-Catalyzed Reactions

34. Figure 6.9 Enzyme and Substrate

35. Figure 6.10 Enzymes Lower the Energy Barrier

36. Figure 6.12 Some Enzymes Change Shape When Substrate Binds to Them: INDUCED FIT

37. Some enzymes require “partners”: Prosthetic groups: Cofactors: Coenzymes:

42. Figure 6.14 Catalyzed Reactions Reach a Maximum Rate

43. 7.6.1 State that metabolic pathways consist of enzyme-catalysed reactions in: Chemical rxns usually multiple steps Each step has own enzyme Chains (glycolysis) Cycles (Krebs, Calvin Cycles)

44. Figure 6.17 Reversible Inhibition – inhibitor & substrate compete for active site

45. Figure 6.17 Reversible Inhibition– inhibitor binds to alternative site (not active site) & changes shape of active site Online Animated Tutorial

46. Figure 6.18 Allosteric Regulation of Enzymes INACTIVE FORMACTIVE FORM Inhibitor site Active site Activator site Catalytic subunit Regulatory subunits The enzyme switches back and forth between the two forms. They are in equilibrium. Online Animated Tutorial

47. Figure 6.18 Allosteric Regulation of Enzymes INACTIVE FORM Allosteric inhibitor Binding of an inhibitor makes it less likely that the active form will occur.