1. Compare and Contrast inorganic and organic molecules Carbon Dioxide (CO2) Glucose (C6H12O6) Water (H2O) Methane (CH4)

2. 4 Major Macromolecules - Proteins Carbohydrates Nucleic acids Lipids These organic molecules comprise approximately 25% of all living organisms !

3. Contrast the terms monomer and polymer Monomers are the building blocks of polymers Ex: Amino Acids -> Proteins (Polypeptides)

4. How do we build and breakdown macromolecules?

6. Monomers: monosaccharides

8. Covalently Joining Monosaccharides together…

9. How does variation in molecular building blocks provide cells with a wider range of functions?

10. Starches—major energy storage molecule in plants Glycogen—major energy storage molecule in animals Cellulose—major structural component of “plant-like” cell walls **These polysaccharides are ALL comprised entirely of glucose monomers**

11. Images of Three Major Polysaccharides

12. How are lipids different from carbohydrates, even though they are composed of the same three elements? Lipids are insoluble in water because of many nonpolar covalent bonds. Widest Variation among molecules Functions…

13. Figure 2.12 Saturated Fatty Acid (Part 1)

14. Figure 2.12 Unsaturated Fatty Acid (Part 2)

15. Explain the difference between a saturated fatty acid and an unsaturated fatty acid. Structure function relationship… Saturated versus Unsaturated Fatty Acids…

16. THINK ABOUT IT: At night, the cotton plant can avoid freezing by increasing the number of unsaturated fatty acids in its cell membranes… How does this enhance its survival?

17. Figure 2.13 B Phospholipids

18. Nucleic Acids: Monomers - Nucleotides 3 components of a Nucleotide:

19. Polymers of Nucleic Acids: Examples!

20. The CENTRAL DOGMA OF BIOLOGY! DNA->RNA->Protein A change in DNA sequence can affect all levels of organism function!

21. Amino Acids: The building blocks of proteins 20 different types in most biological systems Same general structure with a variable “R” group

23. Covalently bonding Amino Acids to form a Protein:

24. The four levels of protein structure – Due to its extreme complexity Primary structure: The sequence of amino acids in a polypeptide chain Interactions: Peptide Bonds

25. Concept 3.2 Proteins Are Polymers with Important Structural and Metabolic Roles Secondary structure – helices and pleated sheet structures seen in proteins Interactions: H-bonds between H of one amino acid and O of nonadjacent a.a.s

26. Concept 3.2 Proteins Are Polymers with Important Structural and Metabolic Roles Tertiary structure: Specific, unique 3D structure of a protein Interactions: R-group interactions between each other and the environment Ex: nonpolar attractions, + and – attractions, hydrophilic interactions with water

27. Figure 3.9 The Structure of a Protein

28. Quarternary Structure Quaternary structure—Structure that results from multiple polypeptide chains interacting (ex: insulin, hemoglobin)

29. Digestive Enzymes!!

30. How can changes in molecular units of proteins result in a wider range of function? Fetal versus Adult hemoglobin:

31. Antibody Diversity

32. Denaturation: Which level of protein structure would be disrupted first? Which level of protein structure would be the hardest to disrupt? Changes in the environment resulting in changes in the 3D structure of a protein -> disrupts function Tertiary disrupted first; Primary hardest to disrupt

33. THINK ABOUT IT: How did this lesson demonstrate the relationship between structure and function of biological molecules? Shape determines function is a MAJOR theme in biology. What determines the shape of these organic compounds?