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Chapter 3 Hw

1. The order in which amino acids are linked in peptides is given


a. from the C-terminal to the N-terminal end
b. from the N-terminal to the C-terminal end
c. in alphabetical order
d. in order of increasing molecular weights of the amino acid residues

2. At its isolectric pH, glycine will have


a. both of its ionizable functional groups dissociated.
b. neither of its ionizable functional groups dissociated.
c. only its carboxyl group dissociated.
d. only its amino group dissociated.

3. The pKa values of the side chains of the common amino acids
a. are always at low pH
b. are always at high pH
c. depend on the chemical nature of the side chain
d. are not known

4. Which of the following correctly describes peptide bonds?


a. They are special type of amide bond.
b. They are a very stable bonds.
c. They are formed when water is split out from an amino group and a carboxylic acid.
d. They are a bond which displays resonance.
e. All of these

5. Which is the C-terminal amino acid in the peptide ALA-GLN-ARG-SER-HIS?


a. ALA
b. GLN
c. ARG
d. SER
e. HIS

6. Which amino acid is classified as polar?


a. L
b. H
c. P
d. I

7. Which amino acid takes on a positive charge when the R-group gains a proton?
a. Glutamic Acid
b. Histidine
c. Glutamine
d. Tyrosine
e. Glycine

8. The net charge on the amino acid cys in a solution at pH 7 is closest to


a. −2
b. −1.
c. 0.
d. +1.

9. Which amino acid has the least polar R-group H?


a. Glutamic Acid
b. Histidine
c. Isoleucine
d. Serine
e. Tyrosine

10. Which of the following amino acids has a net charge of +1 at pH 4 and a net charge of 0 at pH 8?
a. glu
b. arg
c. his
d. tyr

Chapter 4 Home work


1. Quaternary structure is associated with
a. the overall shape of the polypeptide chain
b. the sum of secondary and tertiary interactions
c. simple proteins with only one subunit
d. the relative orientation of one polypeptide to another polypeptide in a multisubunit protein

2. Vitamin C (ascorbic acid) prevents scurvy because


a. it is involved in the formation of the proper β-sheet structure of collagen.
b. it is involved in the metabolism of heme used in hemoglobin.
c. it encourages the formation of disulfide linkages in collagen.
d. it is an unusual amino acid found in the primary structure of collagen.
e. it is used to hydroxylate prolines in the primary structure of collagen.

3. Which of the following proteins is not homologous with the others?


a. myoglogin
b. α-chain of hemoglobin
c. β-chain of hemoglobin
d. collagen

4. Heme would best be described as a


a. motif.
b. domain.
c. prosthetic group.
d. helix.

5. Which of the following is the most common function for fibrous proteins?
a. enzymes
b. structural roles.
c. carrier molecules.
d. enzymes and carrier molecules.
e. All of these.

6. Hydroxyurea works as a treatment for sickle cell anemia because it


a. causes myoglobin to act like hemoglobin
b. causes the body to produce fetal hemoglobin
c. causes hemoglobin to dissociate into monomers, thereby quadrupline the effective
concentration of oxygen carrying molecules
d. none of the choices

7. In the Bohr effect the binding of oxygen to hemoglobin


a. is increased by the presence of Na+
b. is increased by the presence of H+ and CO2
c. is decreased by the presence of H+ and CO2
d. is unchanged

8. Assuming the oligopeptide ALPHAHELICKS forms one continuous α-helix, the carbonyl oxygen of
the glutamic acid residue is hydrogen bonded to the amide nitrogen of
a. leucine.
b. isoleucine.
c. cysteine.
d. lysine.
e. serine.

9. Which of the following best describes what happens when hemoglobin binds bisphosphoglyceric acid
(BPG)?
a. Binding of BPG leads to tighter binding of oxygen.
b. Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.
c. Binding of BPG is important to the allosteric nature of hemoglobin
d. Binding of BPG causes the subunits of hemoglobin to separate.

10. The affinity of fetal hemoglobin for oxygen


a. has not been studied
b. is the same as that of adult hemoglobin
c. is lower than that of maternal hemoglobin
d. is higher than that of maternal hemoglobin

Chapter 5 home work


1. What tends to happen to the percent recovery during a protein's purification?
a. The number usually steadily increases during the purification.
b. The number usually steadily decreases during the purification.
c. The number usually stays fairly constant during the purification.
d. There is no general trend for percent recovery during a protein purification.
ANSWER:

2. Salting out with ammonium sulfate is based upon proteins interacting with other proteins via
a. hydrogen bonds.
b. ionic bonds.
c. hydrophobic interactions.
d. disulfide bonds.
ANSWER:
3. Which of the following are principles on which to base column chromatography?
a. Molecular size
b. Isoionic pH or pI
c. Ion exchange
d. Both molecular size and ion exchange
e. All of these
ANSWER:
4. Which separates on the basis of molecular weight?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANSWER:
5. Elution of proteins by means of a pH gradient would work best with this type of column:
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANSWER:
6. Which would be best to separate proteins of similar size?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANSWER:
7. In the SDS-PAGE (sodium dodecylsulfate - polyacrylamide gel electrophoresis) method, separation
takes place on the basis of
a. charge only, because all particles have different charges, but the same mass.
b. the sieving action of the gel, because all particles have the same charge, but different masses.
c. the sieving action of the gel, because all particles have approximately the same charge/mass
ratio, but different masses.
d. the chemical nature of the buffer used as the electrolyte.
ANSWER:
8. If a protein with the sequence FEWPRQVDMARINE is treated with chymotrypsin, what will the
products be?
a. F EW PRQVMARINE
b. FE WPRQVD MARINE
c. FEWPR QVDMAR INE
d. FEWPRQVDM ARINE
ANSWER:
9. When end-group analysis was done on the protein insulin, the results indicated that both glycine and
phenylalanine were N-terminal amino acids and both asparagine and alanine were C-terminal amino
acids. These results indicate that
a. the experiment was done incorrectly
b. no conclusions can be drawn
c. there were impurities in the sample
d. insulin consists of two polypeptide chains
ANSWER:
10. Which of the following explains why a secondary antibody is used in an ELISA?
a. two antibodies will be twice as visible as one antibody
b. it allows the visible signal to be amplified
c. primary antibodies cannot be tagged with visible markers
d. none of the choices
ANSWER:
11. Studying how proteins interact with other proteins is called
a. expression proteomics
b. structural proteomics
c. interaction proteomics
d. none of the choices
ANSWER: