Chapter 4 Objectives
1. Summarize the philosophies of vitalism and mechanism, and explain how they influenced the development of organic chemistry, as well as mainstream biological thought.
2. Explain how carbon's electron configuration determines the kinds and number of bonds carbon will
3. Describe how carbon skeletons may vary, and explain how this variation contributes to the diversity and complexity of organic molecules.
4. Distinguish among the three types of isomers: structural, geometric and enantiomers.
5. Recognize the major functional groups, and describe the chemical properties of organic molecules in which they occur.
Chapter 5 Objectives
1. List the levels of biological hierarchy from subatomic particles to macromolecules.
2. Explain how organic polymers contribute to biological diversity.
3. Describe how covalent linkages are formed and broken in organic polymers.
4. Describe the distinguishing characteristics of carbohydrates, and explain how they are classified.
5. List four characteristics of a sugar.
6. Identify a glycosidic linkage and describe how it is formed.
7. Describe the important biological functions of polysaccharides.
8. Distinguish between the glycosidic linkages found in starch and cellulose, and explain why the difference is biologically important.
9. Explain what distinguishes lipids from other major classes of macromolecules.
10. Describe the unique properties, building block molecules and biological importance of the three important groups of lipids: fats, phospholipids and steroids.
11. Identify an ester linkage and describe how it is formed.
12. Distinguish between a saturated and unsaturated fat, and list some unique emergent properties that are a consequence of these structural differences.
13. Describe the characteristics that distinguish proteins from the other major classes of macromolecules, and explain the biologically important functions of this group.
14. List and recognize four major components of an amino acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains. 15. Identify a peptide bond and explain how it is formed.
16. Explain what determines protein conformation and why it is important.
17. Define primary structure and describe how it may be deduced in the laboratory.
18. Describe the two types of secondary protein structure, and explain the role of hydrogen bonds in maintaining the structure.
19. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure.
20. Using collagen and hemoglobin as examples, describe quaternary protein structure. 21. Define denaturation and explain how proteins may be denatured.
22. .Describe the characteristics that distinguish nucleic acids from the other major groups of macromolecules
23. Summarize the functions of nucleic acids.
24. List the major components of a nucleotide, and describe how these monomers are linked together to form a nucleic acid.
25. Distinguish between a pyrimidine and a purine.
26. List the functions of nucleotides.
27. Briefly describe the three-dimensional structure of DNA.
Chapter 6 Objectives
I. 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. Explain, in their own words, the First and Second Laws of Thermodynamics.
5. Explain why highly ordered living organisms do not violate the Second 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 useable energy that can be harvested from a reaction.
9. Explain the usefulness of free energy.
10. List two 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 three 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 (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 regulators.
24. Distinguish between allosteric activation and cooperativity.
25. Explain how metabolic pathways are regulated.