AP/IB Biology Study Guide Unit 2
Organic Chemistry (Chapters 4 & 5)
1. Explain how carbon's electron configuration determines the kinds and number of bonds carbon will form
2. Describe how carbon skeletons may vary
3. Explain how the variation in carbon skeleton contributes to the diversity and complexity of organic molecules
4. Distinguish among the three types of isomers: structural, geometric, and enantiomers
5. Recognize and identify the structural formulas for the major functional groups and describe the chemical properties of organic molecules in which they occur
6. List the 4 major classes of biomolecules
7. Explain how organic polymers contribute to biological diversity
8. Describe how covalent linkages are formed and broken in organic polymers
9. Describe the distinguishing characteristics of carbohydrates and explain how they are classified
10. List four characteristics of a sugar and identify the structural formulas of representative mono- and disaccharides
11. Identify a glycosidic linkage and describe how it is formed
12. Describe the important biological functions of polysaccharides
13. Distinguish between the glycosidic linkages found in starch and cellulose and explain why the difference is biologically important
14. Explain what distinguishes lipids from other major classes of macromolecules
15. Identify an ester linkage and describe how it is formed
16. Distinguish between saturated and unsaturated fats and steroid-based lipids and identify the formulas for representative examples
17. Describe the characteristics that distinguish proteins from the other major classes of macromolecules and explain the biologically important functions of proteins
18. List and recognize four components of and amino acid and explain how amino acids may be grouped according to the physical and chemical properties of the side chains
19. Identify the structural formulas of biologically important amino acids
20. Identify a peptide bond and explain how it is formed
21. Explain what determines protein conformation and why it is important
22. Define primary structure and describe how it may be deduced in the laboratory
23. Describe the two types of secondary protein structure and explain the role of hydrogen bonds in maintaining the structure
24. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure
25. Using collagen and hemoglobin as examples, describe quaternary protein structure
26. Define denaturation and explain how proteins may be denatured
27. Describe the characteristics that distinguish nucleic acids from the other major groups of macromolecules
28. Summarize the functions of nucleic acids
29. List the components of a nucleotide and describe how these monomers are linked together to from a nucleic acid
30. Recognize and distinguish between the structural formula of purine and pyrimidine bases
31. Distinguish between the structural formulas of ribose and deoxyribose
32. List the functions of nucleotides
33. Briefly describe the 3-dimenstional structure of DNA
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Metabolism (Chapter 6)
1. Explain the role of catabolic and anabolic pathways in the energy exchanges of cellular metabolism
2. Distinguish between kinetic and potential energy
3. Distinguish between open and closed systems
4. Enunciate and explain the 1st and 2nd Laws of Thermodynamics
5. Explain why highly ordered living systems do not violate the 2nd Law of Thermodynamics
6. Distinguish between entropy and enthalpy
7. Write the Gibbs equation for free energy change
8. Explain how changes in enthalpy, entropy, and temperature influence the maximum amount of usable energy that can be harvested from a reaction
9. Explain the usefulness of free energy
10. List 2 major factors capable of driving spontaneous processes
11. Distinguish between exergonic and endergonic reactions
12. Describe the relationship between equilibrium and free energy change for a reaction
13. Describe the function of ATP in the cell
14. List the 3 components of ATP and identify the major class of macromolecules to which it belongs
15. Explain how ATP performs cellular work
16. Explain why chemical disequilibrium is essential for life
17. Describe the energy profile of a chemical reaction including activation energy (EA), free energy change ( D G), and transition state
18. Describe the function of enzymes in biological systems
19. Explain the relationship between enzyme structure and enzyme specificity
20. Explain the induced fit model of enzyme function and describe the catalytic cycle of an enzyme
21. Describe several mechanisms by which enzymes lower activation energy
22. Explain how substrate concentration affects the rate of an enzyme-controlled reaction
23. Explain how enzyme activity can be regulated or controlled by environmental conditions, cofactors, enzyme inhibitors, and allosteric inhibition
24. Distinguish between allosteric activation and cooperativity
25. Explain how metabolic pathways are regulated
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