Big Picture Study Guide for CHEM 120B Exam Two

Chapter 18

1. From given structures of amino acids be able to:

a) determine whether a side chain is acidic, basic, polar, or nonpolar.
b) determine whether an amino acid is achiral, has one chiral carbon, or has two chiral carbons.
c) show what an amino acid would like at different pH values in reference to its pI.
d) determine what secondary structures an amino acid would likely belong to (hydrophobic pocket, H-bonded
structure such as an α-helix or β-sheet, salt bridge, disulfide bridge)

2. Understand how amino acids form peptide bonds, the properties of peptide bonds, and how a peptide is named.

3. Understand how to determine whether a compound is chiral, whether a pair of compounds are enantiomers,
and the properties of enantiomers that are similar and different.

4. Understand the aspects of primary, secondary, tertiary, and quaternary structure in proteins.

5. Understand the common properties of proteins and the functions of the various classes of proteins (enzymes,
hormones, etc.) Understand that while proteins differ in function, they are all built from the same 20 amino
acids.

6. Understand the differences between fibrous and globular proteins and know common examples of each.

7. Describe the difference between hydrolysis and denaturation and give examples of agents that can cause each
process.

Chapter 19

1. Understand the following terms related to enzymes: active site, substrate, specificity, turnover, cofactor,
coenzyme.

2. List the properties of enzymes that make specificity possible.

3. Given a reaction, identify the class of enzyme that would catalyze that reaction.

4. Describe the changes in enzyme activity that result with changes in substrate concentration, enzyme
concentration, temperature, and pH.

5. Define and identify applications of the following methods of enzyme control: feedback, allosteric control,
competitive inhibition, zymogens, covalent modification, genetic control.

6. Given the structure of a vitamin, determine whether it is water-soluble or fat-soluble. Understand the properties
of water-soluble versus fat-soluble vitamins and understand the general role of vitamins in the diet (but not the
specific function of each individual vitamin).

7. (Actually in chapter 21) Identify the highly reactive oxygen species formed during metabolism, the problems
associated with ROS’s, and how enzymes and antioxidants counteract them.

Chapter 20

1. Know the basic function of each of the following: thyroxine, insulin, vasopression, anti-diuretic hormone,
melatonin, serotonin, dopamine, norepinephrine, epinephrine, testosterone, androsterone, estrone, estradiol,
progesterone, acetylcholine, histamine, antihistamine, endorphins
2. Understand the difference between hormones and neurotransmitters. Give examples of each.

3. Understand the various ways that the hypothalamus can communicate with other tissues.

4. Understand the differences between steroid hormones and protein hormones in terms of structure and ability
to enter the cell.

5. Outline the sequence of events in the action of acetylcholine.

6. Describe how drugs can act as agonists and antagonists. Relate this to the function of acetylcholine. Describe
the concept of drug dependency.

Chapter 21

1. Explain the differences between exergonic and endergonic reactions.

2. Know the big picture of metabolism as diagrammed on page 599, the difference between catabolism and
anabolism, the four stages of metabolism, and the locations of each of these stages in the body.

3. Understand the three major strategies of metabolism: ATP production, coupled reactions, and oxidized and
reduced coenzymes.

4. Explain what happens in each step of the citric acid cycle. Explain the significant outcomes of the citric acid
cycle in terms of products produced.

5. Understand the general sequence of the electron transport chain. Describe oxidative phosphorylation and how
reduced coenzymes are used to produce ATP.

Chapter 28

1. List the sequence of events in the digestion of proteins, and describe the nature of the amino acid pool.

2. Understand the consequences of too little protein intake and too much protein intake. Know the fates of
excess N atoms and excess C atoms in excess protein intake.

3. Define essential and nonessential amino acids.