Chapter 3
Differentiate between primary (1o), secondary (2o),
tertiary (3o) and quaternary (4o) structure
List the forces involved in each of the levels of structure (peptide
and disulfide bonds; hydrophobic effect, hydrogen bond, electrostatic interaction
and metal ion coordination)
Know the kinds of functions proteins play and an example protein for
each
Know the interrelation between the terms apoprotein, holoprotein, and
prosthetic group
Be able to compare and contrast the a-helix
and ß-sheet, as well as collagen triple helix
Know what denaturation is and how common denaturants such as acid and
alcohol work
Be able to sequence a protein (on paper) given the appropriate experimental
data
Be able to discuss the general process of protein purification, and
how techniques such as affinity chromatogaphy are successful
Be able to discuss some ways of classifying proteins (shape, function,
etc.)
Chapter 4
Be able to use the enzyme commission numbering to classify an enzyme
based on seeing the reaction it catalyzes
Be able to list the vitamin form and coenzyme form of several coenzymes,
as well as the type of reaction that the coenzyme is seen
Be able to identify NAD(H), NADP(H) and FAD(H2)
Know the difference between competitive, noncompetitive, and uncompetitive
inhibitors in terms of: location of binding, time of binding, effect
on Km or Vmax, what a Lineweaver-Burk plot looks like ±inhibitor
Be able to discuss the lock-and-key vs. induced fit model of
enzyme specificity
Be able to discuss the ways in which an enzyme can act as catalyst
Know and be able to discuss the factors that affect enzyme rate
List and discuss the means for regulating enzyme activity
Given a Lineweaver-Burk plot, be able to determine Km, Vmax and type
of inhibition
Chapter 7
Be able to identify the bases, given the structures
Be able to differentiate between and describe the structure of base,
nucleoside and nucleotide
Be able to indicate the base-pairing which occurs in DNA and RNA
Be able to describe the predominant physiological form of DNA (B-DNA)
as well as discuss the possible existence of other forms
Be able to discuss the packing of DNA in prokaryote or eukaryote systems
Be able to describe/sketch the structures of mRNA, tRNA, and rRNA
Discuss the action of a restriction enzyme on DNA
Part B.
1. Explain the terms primary structure, secondary structure, tertiary
structure, and quaternary structure. (5 points) Answer
2. Compare and contrast the a-helix, the
ß-sheet, and the collagen triple helix. (5 points) Answer
3. From the following sequence information, deduce the sequence of
the following octadecapeptide (5 points) Answer
Fragment 1 sequence: Trp-Thr-Asn-Glu-Val-Lys
Fragment 2 sequence: Ala-Phe-Arg-Tyr-Ile-Leu-Phe-Cys
Fragment 3 sequence: Gly-Gly-Pro-Met-Ala-Phe-Arg
4. List the forces that determine protein tertiary structure and briefly
discuss each with respect to amino acids involved, strength of the force,
and prevalence. (5 points) Answer
5. The golgi apparatus is an organelle bounded by a single, 5 nm thick
membrane. One of the functions of the golgi is glycoprotein processing.
If a sugar transport protein passes through this membrane with 12 a-helical
passes, how many amino acids of this protein are required to fulfill this
structural role? (5 points) Answer
6. List four of the six functions that proteins play. (4 points)
Answer
7. Which coenzyme would be required to catalyze the following reaction?
(4 points) Answer
8. Identify the following coenzymes. (4 points) Answer
9. What is the source of the following coenzymes (what is the vitamin
from which they are derived) ? (4 points) Answer
Coenzyme A- ____
N5,N10-methylenetetrahydrofolate-____
Biotin- ____
Lipoic Acid- ____
10. If an enzyme has a maximal velocity (Vmax) of 75 µmol·L-1·min-1
and a Michaelis constant (Km) of 1.1 mmol·L-1, what velocity
would you expect the enzyme to have at a substrate concentration of 1.9
mmol·L-1? (5 points) Answer
11. Using the following experimental data, determine (a) the Km of
the enzyme (b) the Vmax of the enzyme, assuming the experimental conditions
are optimized (c) the type of inhibitor used in the study of the catalytic
mechanism. (10 pts) Answer
V, µmol/min V, µmol/min
[S], mM (no inhibitor)
(with inhibitor)
0.05
0.33
0.14
0.10
0.50
0.25
0.20
0.67
0.40
0.40
0.80
0.57
0.50
0.83
0.63
12. The Enzyme Commission (EC) has classified enzymes according to the
type of reaction catalyzed, substrate, product, and type of bond acted
on. List the six major classes of enzymes in this system. (6 points)Answer
13. Roughly sketch a portion of a DNA molecule and indicate its important
structural features. (5 points) Answer
14. Listed below are the structures of Guanine, Adenine, Cytosine and
Thymidine. Indicate the hydrogen bonding that occurs between the appropriate
bases. (5 points) Answer
15. Compare the 3 major types of RNA. (5 points) Answer
16. List the ways in which DNA differs from RNA. (5 points) Answer