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Biochemistry Practice Quiz

Fall 2016
1.

Which of the following is not correct concerning myoglobin?


A)
The globin chain contains an extensive -helix structure.
B)
The heme group is bound to the globin chain by two disulfide bonds to cysteine
residues.
C)
The iron of the heme group is in the Fe+2 oxidation state.
D)
The diameter of the iron ion decreases upon binding to oxygen.
E)
The function of myoglobin is oxygen storage in muscle.

2.

Which of the following is not correct concerning the oxygenation plot of proteins X and
Y shown below?

A)
B)
C)
D)
E)
3.

Protein X exhibits tighter oxygen binding than protein Y.


Protein Y would function as a better transport protein than protein X.
Protein X exhibits cooperative binding, whereas Y does not.
Protein X corresponds to myoglobin, and protein Y corresponds to hemoglobin.
Protein Y contains multiple binding sites.

The structure of normal adult hemoglobin can be described as


A)
a tetramer composed of four myoglobin molecules.
B)
a tetramer composed of two dimers.
C)
a tetramer composed of two 2 and two 2 dimers.
D)
a tetramer composed of two 2 and two 2 dimers.
E)
None of these accurately describe hemoglobin.

4.
In hemoglobin, the iron of the heme is bonded to the four nitrogens of porphyrin and to
the proximal ______________ residue of the globin chain.
5.

2,3-bisphosphoglycerate binds only to the __________________ form of hemoglobin.

6. An enzyme will specifically bind its substrate because of:


(a) a tight lock-and-key binding mechanism.
(b) a high number of hydrophobic amino acids in the center of the protein.
(c) a large number of weak interactions at the active site.
(d) additional nonprotein cofactors.
(e) None of the above.
7. Given are five KM values for the binding of substrates to a particular enzyme. Which has the
strongest affinity ?
(a) 150 mM
(b) 0.15 mM
150 M
(d) 1.5 nM
(e) 15,000 mM
8. In this type of inhibition, the inhibitor can only bind to the ES complex to form an ESI
complex.
(a) competitive
(b) noncompetitive
irreversible
(d) uncompetitive
(e) None of the above.
9. Organic cofactors are referred to as __________________.

10. Salicylate (aspirin) inhibits the catalytic action of glutamate dehydrogenase. Estimate the Vmax and Km in the
presence and absence of this inhibitor. From the data, determine the type of inhibition?

Substrate, mM
1.5
2.0
3.0
4.0
8.0
16.0

Product per minute (microgram)


no inhibitor
0.21
0.25
0.28
0.33
0.44
0.40

40 mM salicylate (Inhibitor)
0.08
0.1
0.12
0.13
0.16
0.18