1. Figure 5.0 Spider’s web made of protein

2. Figure 5.1 Building models to study the structure and function of macromolecules

3. Figure 5.2 The synthesis and breakdown of polymers

4. Figure 5.3 The structure and classification of some monosaccharides

5. Figure 5.29 The components of nucleic acids; differences between DNA and RNA

6. Figure 5.3x Hexose sugars Glucose Galactose

7. Figure 5.4 Linear and ring forms of glucose

8. Figure 5.5 Examples of disaccharide synthesis

9. Figure 5.5x Glucose monomer and disaccharides Glucose monomer Sucrose Maltose

10. Figure 5.6 Storage polysaccharides

11. Figure 5.7a Starch and cellulose structures

12. Figure 5.7b,c Starch and cellulose structures

13. Figure 5.7x Starch and cellulose molecular models  Glucose  Glucose Starch Cellulose

14. Figure 5.8 The arrangement of cellulose in plant cell walls

15. Figure 5.x1 Cellulose digestion: termite and Trichonympha

16. Figure 5.x2 Cellulose digestion: cow

17. Figure 5.9 Chitin, a structural polysaccharide: exoskeleton and surgical thread

19. Figure 5.10 The synthesis and structure of a fat, or triacylglycerol

20. Figure 5.11x Saturated and unsaturated fats and fatty acids: butter and oil

21. Figure 5.11 Examples of saturated and unsaturated fats and fatty acids

22. Figure 5.12 The structure of a phospholipid

23. Figure 5.13 Two structures formed by self-assembly of phospholipids in aqueous environments

25. Figure 5.14 Cholesterol, a steroid

26. Figure 8.6 The detailed structure of an animal cell’s plasma membrane, in cross section

27. Figure 4.8 A comparison of functional groups of female (estradiol) and male (testosterone) sex hormones

28. Table 5.1 An Overview of Protein Functions

29. Figure 5.0 Spider’s web made of protein

30. Figure 5.15 The 20 amino acids of proteins: nonpolar

31. Figure 5.15 The 20 amino acids of proteins: polar and electrically charged

32. Figure 5.16 Making a polypeptide chain

33. Figure 5.18 The primary structure of a protein

34. Figure 5.20 The secondary structure of a protein

35. Figure 5.22 Examples of interactions contributing to the tertiary structure of a protein

36. Figure 5.17 Conformation of a protein, the enzyme lysozyme

37. Figure 5.23 The quaternary structure of proteins

38. Figure 5.19 A single amino acid substitution in a protein causes sickle-cell disease

39. LE 5-21b Primary structure Secondary and tertiary structures 1 2 3 Normal hemoglobin Val His Leu 4 Thr 5 Pro 6 Glu 7 Primary structure Secondary and tertiary structures 1 2 3 Sickle-cell hemoglobin Val His Leu 4 Thr 5 Pro 6 ValGlu 7 Quaternary structure Normal hemoglobin (top view)         Function Molecules do not associate with one another; each carries oxygen. Quaternary structure Sickle-cell hemoglobin Function Molecules interact with one another to crystallize into a fiber; capacity to carry oxygen is greatly reduced. Exposed hydrophobic region  subunit

40. Figure 5.24 Review: the four levels of protein structure

41. Figure 5.25 Denaturation and renaturation of a protein

42. Figure 5.26 A chaperonin in action

43. Figure 5.x3 James Watson and Francis Crick

44. Figure 5.28 DNA  RNA  protein: a diagrammatic overview of information flow in a cell

45. Figure 5.29 The components of nucleic acids; differences between DNA and RNA

46. Figure 5.30 The DNA double helix and its replication

47. Figure 5.x4 Rosalind Franklin

48. Table 5.2 Polypeptide Sequence as Evidence for Evolutionary Relationships