Biochemistry Flashcards

1
Q

In a neutral solution, most amino acids exist as:
A. positively charged compounds.
B. zwitterions.
C. negatively charged compounds.
D. hydrophobic molecules.

A

B. Zwitterions
Most amino acids (except the acidic and basic amino acids) have two sites for protonation: the carboxylic acid and the amine. At neutral pH, the carboxylic acid will be deprotonated (-COO-) and the amine will remain protonated (-NHz+).
This dipolar ion is a zwitterion, so (B) is the correct answer.

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2
Q

At pH 7, the charge on a glutamic acid molecule IS:
A. -2.
B. -1.
C. 0.
D. +1.

A

B. -1
Glutamic acid is an acidic amino acid because it has an extra carboxyl group. At neutral pH, both carboxyl groups are deprotonated and thus negatively charged. The amino group has a positive charge because it remains protonated at pH 7. Overall, therefore, glutamic acid has a net charge of -1, and (B) is correct. Notice that you do not even need to know the pI values to solve this question; as an acidic amino acid, glutamic acid must have a pI below 7.

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3
Q

Which of the following statements is most likely to be true of nopolar R groups in aqueous solution?
A. They are hydrophilic and found buried within proteins.
B. They are hydrophilic and found on protein surfaces.
C. They are hydrophobic and found buried within proteins.
D. They are hydrophobic and found on protein surface

A

C. They are hydrophobic and found buried within proteins.
Nonpolar groups are not capable of forming dipoles or hydrogen bonds; this makes them hydrophobic. Burying hydrophobic R groups inside proteins means they don’t have to interact with water, which is polar. This makes (C) correct. (A) and (B) are incorrect because nopolar molecules are hydrophobic, not hydrophilic; (D) is incorrect because they are not generally found on protein surfaces.

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4
Q

Scientists discover a DNA sequence for an uncharacterized protein. In their initial studies, they use a computer program designed to predict protein structure. Which of the following levels of protein structure can be most accurately predicted?
A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure

A

A. Primary structure
The cDNA sequence is a DNA copy of the mRNA used to generate a protein. A computer program can quickly identify the amino acid that corresponds to each codon and generate a list of these amino acids. This amino acid sequence is the primary structure of the protein. These observations support
(A) as the correct answer. By contrast, the secondary, tertiary, and quaternary structures involve higher level interactions between the backbone and R groups and are increasingly difficult to predict.

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5
Q

How many distinct tripeptides can be formed from one valine molecule, one alanine molecule, and one
leucine molecule?
A. 1
B. 3
C. 6
D. 27

A

C. 6
There are three choices for the first amino acid, leaving two choices for the second, and one choice for the third.
Multiplying those numbers gives us a total of 3 x 2 x 1 = 6
distinct tripeptides. (Using the one-letter codes for valine (V), alanine (A), and leucine (L), those six tripeptides are VAL, VLA, ALV, AVL, LVA, and LAV.)

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6
Q

Which of the following best describes the change in entropy that occurs during protein folding?
A. Entropy of both the water and the protein increase.
B. Entropy of the water increases; entropy of the protein decreases.
C. Entropy of the water decreases; entropy of the protein increases.
D. Entropy of both the water and the protein decrease.

A

B
As the protein folds, it takes on an organized structure and thus its entropy decreases. However, the opposite trend is true for the water surrounding the protein. Prior to protein folding, hydrophobic amino acid residues are exposed and the water molecules must form structured hydration shells around these hydrophobic residues. During fold-ing, these hydrophobic residues are generally buried in the interior of the protein so that the surrounding water molecules gain more latitude in their interactions. Thus, the entropy of the surrounding water increases, making the correct answer (B).

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7
Q

An α-helix is most likely to be held together by:
A. disulfide bonds.
B. hydrophobic effects.
C. hydrogen bonds.
D. ionic attractions between side chains.

A

C. Hydrogen bonds
The α-helix is held together primarily by hydrogen bonds between the carboxyl groups and amino groups of amino acids. Disulfide bridges, (A), and hydrophobic effects, (B), are primarily involved in tertiary structures, not secondary.
Even if they were charged, the side chains of amino acids are too far apart to participate in strong interactions in secondary structure.

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8
Q

Which of the following is least likely to cause denaturation of proteins?
A. Heating the protein to 100°C
B. Adding 8 M urea
C. Moving it to a more hypotonic environment
D. Adding a detergent such as sodium dodecyl sulfate

A

C. Moving it to a more hypotonic environment
High salt concentrations and detergents can denature a protein, as can high temperatures. But moving a protein to a hypotonic environment-that is, a lower solute concentration-should not lead to denaturation.

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9
Q

A particular α-helix is known to cross the cell membrane. Which of these amino acids is most likely to be found in the transmembrane portion of the helix?
A. Glutamate
B. Lysine
C. Phenylalanine
D. Aspartate

A

C. Phenylalanine
An amino acid likely to be found in a transmembrane portion of an α-helix will be exposed to a hydrophobic environment, so we need an amino acid with a hydrophobic side chain. The only choice that has a hydrophobic side chain is (C), phenylalanine. The other choices are all polar or charged.

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10
Q

Which of these amino acids has a chiral carbon in
its side chain?
I. Serine
Il. Threonine
Ill. Isoleucine
A. I only
B. Il only
C. Il and Ill only
D. I, II, and III

A

C. II and III only
Every amino acid except glycine has a chiral a-carbon, but only two of the 20 amino acids— threonine and isoleucine— also have a chiral carbon in their side chains as well. Thus, the correct answer is (C). Just as only one configuration is normally seen at the a carbon, only one configuration is seen in the side chain chiral carbon.

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11
Q

Following translation and folding, many receptor tyrosine kinases exist as monomers in their inactive state on the cell membrane. Upon the binding of a ligand, these proteins dimerize and initiate a signaling cascade. During this process, their highest element of protein structure changes from:
A. secondary to tertiary.
B. tertiary to quaternary.
C. primary to secondary.
D. secondary to quaternary.

A

B. tertiary to quaternary
In their inactive state, the receptor tyrosine kinases are fully folded single polypeptide chains and thus have tertiary struc-ture. When these monomers dimerize, they become a protein complex and thus have elements of quaternary structure. This change from tertiary to quaternary structure justifies (B).

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12
Q

Which of these amino acids has a side chain that can become ionized in cells?
A. Histidine
B. Leucine
C. Proline
D. Threonine

A

A. Histidine
Histidine has an ionizable side chain: its imidazole ring has a nitrogen atom that can be protonated. None of the remaining answers have ionizable atoms in their side chains.

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13
Q

In lysine, the pka of the side chain is about 10.5.
Assuming that the pK, of the carboxyl and amino groups are 2 and 9, respectively, the pl of lysine is closest to:
A. 5.5.
B. 6.2.
C. 7.4.
D. 9.8.

A

D. 9.8
Because lysine has a basic side chain, we ignore the pK, of the carboxyl group, and average the pK of the side chain and the amino group; the average of 9 and 10.5 is 9.75, which is closest to (D).

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14
Q

Which of the following is a reason for conjugating proteins?
I. To direct their delivery to a particular organelle
Il. To direct their delivery to the cell membrane
III. To add a cofactor needed for their activity
A. I only
B. II only
C. Il and Ill only
D. I, Il, and III

A

D. I, II, III
Conjugated proteins can have lipid or carbohydrate “tags” added to them. These tags can indicate that these proteins should be directed to the cell membrane (especially lipid tags) or to specific organelles (such as the lysosome). They can also provide the activity of the protein; for example, the heme group in hemoglobin is needed for it to bind oxygen.
Thus, (D) is the correct answer.

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15
Q

Collagen consists of three helices with carbon backbones that are tightly wrapped around one another in a “triple helix.” Which of these amino acids is most likely to be found in the highest concentration in collagen?
A. Proline
B. Glycine
C. Threonine
D. Cysteine

A

B. Glycine
Because collagen has a triple helix, the carbon backbones are very close together. Thus, steric hindrance is a potential problem. To reduce that hindrance, we need small side chains; glycine has the smallest side chain of all: a hydrogen atom.

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16
Q

Consider a biochemical reaction A → B, which is catalyzed by A-B dehydrogenase. Which of the following statements is true?
A. The reaction will proceed until the enzyme concentration decreases.
B. The reaction will be most favorable at 0°C.
C. A component of the enzyme is transferred from A to B.
D. The free energy change (dG) of the catalyzed reaction is the same as for the uncatalyzed reaction.

A

D. The free energy change (dG) of the catalyzed reaction is the same as for the uncatalyzed reaction.
Enzymes catalyze reactions by lowering their activation energy, and are not changed or consumed during the course of the reaction. While the activation energy is lowered, the free energy of the reaction, dG, remains unchanged in the presence of an enzyme. A reaction will continue to occur in the presence or absence of an enzyme; it simply runs slower without the enzyme, eliminating (A). Most physiological reactions are optimized at body temperature, 37°C, eliminating (B). Finally, dehydrogenases catalyze oxidation-reduction reactions, not transfer reactions, eliminating (C).

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17
Q

Which of the following statements about enzyme kinetics is FALSE?
A. An increase in the substrate concentration (at constant enzyme concentration) leads to proportional increases in the rate of the reaction.
B. Most enzymes operating in the human body work best at a temperature of 37°C.
C. An enzyme-substrate complex can either form a product or dissociate back into the enzyme and substrate.
D. Maximal activity of many human enzymes occurs around pH 7.4.

A

A. An increase in the substrate concentration (at constant enzyme concentration) leads to proportional increases in the rate of the reaction.
Most enzymes in the human body operate at maximal activity around a temperature of 37°C and a pH of 7.4, which is the pH of most body fluids. In addition, as characterized by the Michaelis-Menten equation, enzymes form an enzyme-substrate complex, which can either dissociate back into the enzyme and substrate or proceed to form a product. So far, we can eliminate (B), (C), and (D), so let’s check (A). An increase in the substrate concentration, while maintaining a constant enzyme concentration, leads to a proportional increase in the rate of the reaction only initially. However, once most of the active sites are occupied, the reaction rate levels off, regardless of further increases in substrate con-centration. At high concentrations of substrate, the reaction rate approaches its maximal velocity and is no longer changed by further increases in substrate concentration.

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18
Q

Some enzymes require the presence of a nonprotein molecule to behave catalytically. An enzyme devoid of this molecule is called a(n):
A. holoenzyme.
B. apoenzyme.
C. coenzyme.
D. zymoenzyme.

A

B. Apoenzyme
An enzyme devoid of its necessary cofactor is called an apoenzyme and is catalytically inactive.

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19
Q

Which of the following factors determine an enzyme’s specificity?
A. The three-dimensional shape of the active site
B. The Michaelis constant
C. The type of cofactor required for the enzyme to be active
D. The prosthetic group on the enzyme

A

A. The three-dimensional shape of the active site
An enzyme’s specificity is determined by the three-dimensional shape of its active site. Regardless of which explanation for enzyme specificity we are discussing (lock and key or induced fit), the active site determines which substrate the enzyme will react with.

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20
Q

Human DNA polymerase is removed from the freezer and placed in a 60°C water bath. Which of the following best describes the change in enzyme activity
as the polymerase sample comes to
thermal equilibrium with the water bath?
A. Increases then decreases
B. Decreases then plateaus
C. Increases then plateaus
D. Decreases then increases

A

А. Increases then decreases
As the temperature of the DNA polymerase sample increases from 0°C to the usual physiological temperature, i.e. 37°C, the enzyme’s activity will increase. However, at temperatures above 37°C, the enzyme’s activity will rapidly decline due to denaturation.

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21
Q

in the equation below, substrate C is an allosteric inhibitor to enzyme 1. Which of the following is another mechanism necessarily caused by substrate C?

A. Competitive inhibition
B. Irreversible inhibition
C. Feedback enhancement
D. Negative feedback

A

D. Negative feedback
By limiting the activity of enzyme 1, the rest of the pathway is slowed, which is the definition of negative feedback. (A) is incorrect because there is no competition for the active site with allosteric interactions. While many products do indeed competitively inhibit an enzyme in the pathway that creates them, this is an example of an allosterically inhibited enzyme. There is not enough information for (B) to be correct because we aren’t told whether the inhibition is reversible. In general, allosteric interactions are temporary.
(C) is incorrect because it is the opposite of what occurs when enzyme 1 activity is reduced.

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22
Q

The activity of an enzyme is measured at several different substrate concentrations, and the data are shown in the table below.

Km for this enzyme is approximately:
A. 0.5
B. 1.0
C. 10.0
D. 50.0

A

A. 0.5
While the equations given in the text are useful, recognizing relationships is even more important. You can see that as substrate concentration increases significantly, there is only a small change in the rate. This occurs as we approach Vmax Because the Vmax is near 100mmol/min, Vmax/2 equals 50mmol/min. The substrate concentration giving this rate is 0.5mM and corresponds to K; therefore, (A) is correct.

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23
Q

Consider a reaction catalyzed by enzyme A with a Km value of 5 x 10^-6 M and Vmax of 20 mmol
8. At a concentration of 5 x 10^-6 M substrate, the rate of the reaction will be:
A. 10 mmol/min
B. 20 mmol/min
C. 30 mmol/min
D. 40 mmol/min

A

А. 10mmol/min
As with the last question, relationships are important. At a concentration of 5 x 10^-6 M, enzyme A is working at one-half of its max because the concentration is equal to the Km of the enzyme. Therefore, one-half of 20 mmol/min is 10 mmol/min which corresponds to (A).

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24
Q

Consider a reaction catalyzed by enzyme A with a Km value of 5 x 10^-6 M and Vmax of 20 mmol/min

At a concentration of 5 x 10^-4 M substrate, the rate of the reaction will be:
A. 10 mmol/min
B. 15 mmol/min
C. 20 mmol/min
D. 30 mmol/min

A

C. 20 mmol/min
At a concentration of 5 × 10^-4 M, there is 100 times more substrate than present at half maximal velocity. At high values (significantly larger than the value of Km), the enzyme is at or near its max, which is 20 mmol/min

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25
Q

The graph below shows kinetic data obtained for flu virus enzyme activity as a function of substrate concentration in the presence and absence of two antiviral drugs.

Based on the graph, which of the following statements is correct?
A. Both drugs are noncompetitive inhibitors of the viral enzyme.
B. Oseltamivir increases the Km value for the substrate compared to Relenza.
C. Zanamivir increases the Vmax Value for the substrate compared to Tamiflu.
D. Both drugs are competitive inhibitors of the viral enzyme.

A

B
Based on the graph, when the substrate is present, oseltamivir results in the same Vmax and a higher Km, compared to when no inhibitor is added. These are hallmarks of competitive inhibitors. Noncompetitive inhibitors result in decreased Vmax and the same Km, as the uninhibited reaction, which is shown by the zanamivir line in the graph. Because the question is only comparing the values between the two inhibitors, and not the enzyme without inhibitor, the mechanism of inhibition is less important to determine than the values of Km, and Vmax. This is a great example of why previewing the answer choices works well in the sciences.

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26
Q

The conversion of ATP to cyclic AMP and inorganic phosphate is most likely catalyzed by which class of enzyme?
A. Ligase
B. Hydrolase
C. Lyase
D. Transferase

A

C. Lyase
Lyases are responsible for the breakdown of a single molecule into two molecules without the addition of water or the transfer of electrons. Lyases often form cyclic compounds or double bonds in the products to accommodate this. Water was not a reactant, and no cofactor was men-tioned; thus lyase, (C), remains the best answer choice.

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27
Q

Which of the following is NOT a method by which enzymes decrease the activation energy for biological reactions?
A. Modifying the local charge environment
B. Forming transient covalent bonds
C. Acting as electron donors or receptors
D. Breaking bonds in the enzyme irreversibly to provide energy

A

D. Breaking bonds in the enzyme irreversibly to provide energy

Enzymes are not altered by the process of catalysis. A molecule that breaks intramolecular bonds to provide activation energy would not be able to be reused.

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28
Q

A certain enzyme that displays positive cooperativity has four subunits, two of which are bound to substrate. Which of the following statements must be true?
A.
The affinity of the enzyme for the substrate has just increased.
B. The affinity of the enzyme for the substrate has just decreased.
C. The affinity of the enzyme for the substrate is half of what it would be if four sites had substrate bound.
D. The affinity of the enzyme for the substrate is greater than with one substrate bound.

A

D. The affinity of the enzyme for the substrate is greater than with one substrate bound.
Cooperative enzymes demonstrate a change in affinity for the substrate depending on how many substrate molecules are bound and whether the last change was accomplished because a substrate molecule was bound or left the active site of the enzyme. Because we cannot determine whether the most recent reaction was binding or dissociation, (A) and (B) are eliminated. We can make absolute comparisons though. For enzymes expressing positive cooperativity, the unbound enzyme has the lowest affinity for substrate, and the enzyme with all but one subunit bound has the highest.
The increase in affinity is not necessarily linear. Further-more, if all four sites have substrate bound, the enzyme cannot bind to any more substrate. Therefore, (C) is not true. An enzyme with two subunits occupied must have a higher affinity for the substrate than the same enzyme with only one subunit occupied; thus, (D) is correct.

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29
Q

Which of the following is LEAST likely to be required for a series of metabolic reactions?
A. Triacyglycerol acting as a coenzyme
B. Oxidoreductase enzymes
C. Magnesium acting as a cofactor
D. Transferase enzymes

A

А. Triacyglycerol acting as a coenzyme
Triglycerides are unlikely to act as coenzymes for a few reasons, including their large size, neutral charge, and ubig-uity in cells. Cofactors and coenzymes tend to be small in size, such as metal ions like (C) or small organic molecules.
They can usually carry a charge by ionization, protonation, or deprotonation. Finally, they are usually in low, tightly regulated concentrations within cells. Metabolic pathways would be expected to include both oxidation-reduction reactions and movement of functional groups, thus eliminating (B) and (D).

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30
Q

How does the ideal temperature for a reaction change with and without an enzyme catalyst?
A. The ideal temperature is generally higher with a catalyst than without.
B. The ideal temperature is generally lower with a catalyst than without.
C. The ideal temperature Is characteristic of the reaction, not the enzyme.
D. No conclusion can be made without knowing the enzyme type.

A

B. The ideal temperature is generally lower with a catalyst than without.
The rate of reaction increases with temperature because of the increased kinetic energy of the reactants, but reaches a peak temperature because the enzyme denatures with the disruption of hydrogen bonds at excessively high temperatures. In the absence of enzyme, this peak temperature is generally much hotter. Heating a reaction provides molecules with an increased chance of achieving the activation energy, but the enzyme catalyst would typically reduce activation energy. Keep in mind that thermodynamics and kinetics are not interchange-able, so we are not considering the impact of heat on the equilibrium position.

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31
Q

At what pH can protein A best be obtained through electrophoresis? (Note: MM = molar mass)

A. 2.5
В. 3.5
С. 4.5
D. 5.5

A
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32
Q

What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE?
A. SDS stabilizes the gel matrix, improving resolution during electrophoresis.
B. SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size.
C. SDS raises the pH of the gel, separating multiunit proteins into individual subunits.
D. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.

A
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33
Q

Which of the following is NOT involved in cell migration?
A. Dynein
B. Flagella
C. Actin
D. Centrioles

A
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34
Q

Which of the following proteins is most likely to be found extracellularly?
A. Tubulin
B. Myosin
C. Collagen
D. Actin

A
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35
Q

Hormones are found in the body in very low concentrations, but tend to have a strong effect.
What type of receptor are hormones most likely to act on?
I. Ligand-gated ion channels
II. Enzyme-linked receptors
III. G protein-coupled receptors
A. I only
B. III only
C. Il and III only
D. I, II, and III

A

C. II and III only
For a ligand present in low quantities to have a strong action, we expect it to initiate a second messenger cascade system. Second messenger systems amplify signals because enzymes can catalyze a reaction more than once while they are active, and often activate other enzymes. Both enzyme-linked receptors and G protein-coupled receptors use second messenger systems, while ion channels do not.

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36
Q

Which of the following is most likely to be found bound to a protein in the body?
A. Sodium
B. Potassium
C. Chloride
D. Calcium

A
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37
Q

Which of the following characteristics is NOT attributed to antibodies?
A. Antibodies bind to more than one distinct antigen.
B. Antibodies label antigens for targeting by other immune cells.
C. Antibodies can cause agglutination by interaction with antigen.
D. Antibodies have two heavy chains and two light chains.

A
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38
Q

Which ion channels are responsible for maintaining the resting membrane potential?
A. Ungated channels
B. Voltage-gated channels
C. Ligand-gated channels
D. No ion channels are involved in maintenance of the resting membrane potential.

A
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39
Q

Which of the following is NOT a component of all trimeric G proteins?
A. Gα
B. Gβ
C. Gγ
D. Gi

A

D. Gi
All trimeric G proteins have a, B, and y subunits-(A), (B), and (C), respectively. Gs, Gi, and Gq are subtypes of the Gα subunit of the trimeric G protein and differ depending on the G protein-coupled receptor’s function.

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40
Q

Which of the following methods would be best to separate large quantities of the following proteins? (Note: MM = molar mass)

A. Ion-exchange chromatography
B. Size-exclusion chromatography
C. Isoelectric focusing
D. Native PAGE

A

B. Size-exclusion chromatography
The proteins described in the question differ primarily in their molecular weights. Their pI values are very close, so ion-exchange chromatography, (A), is not a good choice. The question specifies a large quantity, which is better processed through chromatography than through electrophoresis- (C) and D) —because the gel can only handle a small volume of protein.

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41
Q

Which amino acids contribute most significantly to the pl of a protein?
I. Lysine
Il. Glycine
III. Arginine
A. I only
B. I and II only
C. I and III only
D. Il and III only

A

C. I and III only
The overall pl of a protein is determined by the relative number of acidic and basic amino acids. The basic amino acids are arginine, lysine, and histidine, and the acidic amino acids are aspartic acid and glutamic acid. Glycine’s side chain is a hydrogen atom, so it will have the least contribution of all the amino acids.

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42
Q

How does the gel for isoelectric focusing differ from the gel for traditional electrophoresis?
A. Isoelectric focusing uses a gel with much larger pore sizes to allow for complete migration.
B. Isoelectric focusing uses a gel with SDS added to encourage a uniform negative charge.
C. Isoelectric focusing uses a gel with a pH gradient that encourages a variable charge.
D. The gel is unchanged in isoelectric focusing; the protein mixture is treated before loading.

A

C
The gel in isoelectric focusing uses a pH gradient. When a protein is in a region with a pH above its pl, it is negatively charged and moves toward the anode. When it is in a pH region below its pI, it is positively charged and moves toward the cathode. When the pH equals the pI, the migration of the protein is halted.

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43
Q

Which protein properties allow UV spectroscopy to be used as a method of determining concentration?
A. Proteins have partially planar characteristics in peptide bonds.
B. Globular proteins cause scattering of light.
C. Proteins contain aromatic groups in certain amino acids.
D. All organic macromolecules can be assessed with
UV spectroscopy.

A

C. Proteins contain aromatic groups in certain amino acids.
UV spectroscopy is best used with conjugated systems of double bonds. While the double bond in the peptide bond does display resonance, this is not adequate for UV absorp-tion. However, aromatic systems are conjugated, and phe-nylalanine, tyrosine, and tryptophan all contain aromatic ring structures.

44
Q

A protein collected through affinity chromatography
displays no activity even though it is found to have a high concentration using the Bradford protein assay. What best explains these findings?
A. The Bradford reagent was prepared incorrectly.
B. The active site is occupied by free ligand.
C. The protein is bound to the column.
D. The protein does not catalyze the reaction of interest.

A

B. The active site is occupied by free ligand.
Protein activity and concentration are generally correlated.
Because we have a high concentration of protein, we expect a high activity unless the protein has been damaged or inactivated in some way. The protein could have been inactivated by experimental conditions like detergents, heat, or pH; however, these are not answer choices. Rather, we must consider how the experimental procedure works. Protein elutes off of an affinity column by binding free ligand. In this situation, the binding may not have been reversed and thus the free ligand competes for the active site of the enzyme, lowering its activity.

45
Q

What property of protein-digesting enzymes allows for a sequence to be determined without fully degrading the protein?
A. Selectivity
B. Sensitivity
C. Turnover
D. Inhibition

A

A. Selectivity
The selective cleavage of proteins by digestive enzymes allows fragments of different lengths with known amino acid endpoints to be created. By cleaving the protein with several different enzymes, a basic outline of the amino acid sequence can be created.

46
Q

When glucose is In a straight-chain formation, it:
A. is an aldoketose.
B. is a pentose.
C. has five chiral carbons.
D. is one of a group of 16 stereoisomers.

A

D. is one of a group of 16 stereoisomers.
Glucose is an aldohexose, meaning that it has one aldehyde group and six carbons. Given this information, (A) and
(B) can be eliminated. In aldose sugars, each nonterminal carbon is chiral. Therefore, glucose has four chiral centers, not five, as mentioned in (C). The number of stereoisomers possible for a chiral molecule is 2”, where n is the number of chiral carbons. Because glucose has four chiral centers,
there are 24 = 16 possible stereoisomers.

47
Q

All of the following are true of epimers EXCEPT:
A. they differ in configuration about only one carbon.
B. they usually have slightly different chemical and physical properties.
c. they are diastereomers (with the exception of glyceraldehyde).
D. they have equal but opposite optical activities.

A

D. they have equal but opposite optical activities.
Epimers are monosaccharide diastereomers that differ in their configuration about only one carbon. As with all diastereo-mers, epimers have different chemical and physical proper-ties, and their optical activities have no relation to each other.
Enantiomers have equal but opposite optical activities. There-fore, (D) is the only statement that does not apply to epimers.

48
Q

Aldonic acids are compounds that:
A. can be oxidized, and therefore act as reducing agents.
B. can be reduced, and therefore act as reducing agents.
C. have been oxidized, and have acted as reducing agents.
D. have been oxidized, and have acted as oxidizing agents.

A

C. have been oxidized, and have acted as reducing agents.
Aldonic acids form after the aldehyde group on a reducing sugar reduces another compound, becoming oxidized in the process.

49
Q

The formation of a-d-glucopyranose from
B-D-glucopyranose is called:
A. glycosidation.
B. mutarotation.
C. enantiomerization.
D. racemization.

A

B. mutarotation
Mutarotation is the interconversion between anomers of a compound. Enantiomerization and racemization, (C) and (D), are related: enantiomerization is the formation of a mirror-image or optically inverted form of a compound, whereas racemization is moving a solution toward an equal concentration of both enantiomers. Glycosidation, (A), is the addition of a sugar to another compound.

50
Q

Ketose sugars may have the ability to act as reducing sugars. Which process explains this?
A. Ketose sugars undergo tautomerization.
B. The ketone group is oxidized directly.
C. Ketose sugars undergo anomerization.
D. The ketone group is reduced directly.

A

A. Ketose sugars undergo tautomerization.
Ketose sugars undergo tautomerization, a rearrangement of bonds, to undergo keto-enol shifts. This forms an aldose, which then allows them to act as reducing sugars. A ketone group alone cannot be oxidized. Anomerization, mentioned in (C), refers to ring closure of a monosaccharide, creating an anomeric carbon.

51
Q

What is the product of the following reaction?

A

B.
When glucose reacts with methanol under acid catalysis, the hemiacetal is converted to an acetal via replacement of the anomeric hydroxyl group with an alkoxy group. The result is a type of acetal known as a glycoside. This corresponds with (B). The other choices all show alkoxy groups on the wrong carbon, or too many carbons.

52
Q

Which of the following enzymes cleaves polysaccharide chains and yields maltose exclusively?
A. α-Amylase
B. β-Amylase
c. Debranching enzyme
D. Glycogen phosphorylase

A

B. β-Amylase
β-Amylase cleaves amylose at the nonreducing end of the polymer to yield maltose exclusively, while a-amylase, (A), cleaves amylose anywhere along the chain to yield short polysaccharides, maltose, and glucose. Debranching enzyme, (C), removes oligosaccharides from a branch in glycogen or starches, while glycogen phosphorylase, (D), yields glucose 1-phosphate.

53
Q

When the following straight-chain Fischer projection is converted to a chair or ring conformation, its structure will be:

A

C.
Start by drawing out the Haworth projection. Recall that all the groups on the right in the Fischer projection will go on the bottom of the Haworth projection, and all the groups on the left will go on the top. Next, draw the chair structure, with the oxygen in the back right corner. Label the carbons in the ring 1 through 5, starting from the oxygen and moving clockwise around the ring. Now, draw in the lines for all the axial substituents, alternating above and below the ring.
Remember to start on the anomeric C-1 carbon, where the axial substituent points down. Now start filling in the substituents. The substituent can be in either position on the anomeric carbon, so skip that one for now. The -OH groups on C-2 and C-4 should point downward while the
-OH group on C-3 should point upward; (C), the B-anomer of D-glucose, is the only one that matches.

54
Q

Why is the α-anomer of D-glucose less likely to form than the β-anomer?
A. The β-anomer is preferred for metabolism.
B. The β-anomer undergoes less electron repulsion.
C. The α-anomer is the more stable anomer.
D. The α-anomer forms more in L-glucose.

A

B. The β-anomer undergoes less electron repulsion.
The hydroxyl group on the anomeric carbon of the β-anomer is equatorial, thereby creating less nonbonded strain than the α-anomer, which has the hydroxyl group of the anomeric carbon in axial position.

55
Q

Which two polysaccharides share all of their glycosidic linkage types in common?
A. Cellulose and amylopectin
B. Amylose and glycogen
C. Amylose and cellulose
D. Glycogen and amylopectin

A

D. Glycogen and amylopectin
Glycogen and amylopectin are the only polysaccharide forms that demonstrate branching structure, making them most similar in terms of linkage. Both glycogen and amylopectin use a-1,4 and a-1,6 linkages. Cellulose uses B-1,4 linkages and amylose does not contain a-1,6 linkages.

56
Q

Which of the following is digestible by humans and Is made up of only one type of monosaccharide?
A. Lactose
B. Sucrose
C. Maltose
D. Cellobiose

A

C. Maltose
While maltose and cellobiose both have the same glucose subunits, only maltose is digestible by humans because the β-glycosidic linkages in cellobiose cannot be cleaved in the human body.

57
Q

The reaction below is an example of one step in:

A. aldehyde formation.
B. hemiketal formation.
C. mutarotation.
D. glycosidic bond cleavage.

A

C
In solution, the hemiacetal ring of glucose will break open spontaneously and then re-form. When the ring is broken, bond rotation occurs between C-1 and C-2 to produce either the a- or the B-anomer. The reaction given in this question depicts the mutarotation of glucose. (A) is incorrect because the reactant is an aldehyde, not the product.
(B) is incorrect because a hemiketal has an - OH group, an -OR group, and two - R groups. In addition, hemike-tals are formed from ketones, and our starting reactant is an aldehyde. Finally, (D) is incorrect because there is no glycosidic bond in the starting reactant.

58
Q

Galactose is the C-4 epimer of glucose, the structure of which is shown below. Which of the following structures is galactose?

A

A
Galactose is a diastereomer of glucose, with the stereochemistry at C-4 (counting from the aldehyde) reversed.
Being able to identify C-4 is enough to answer this ques-tion, even without looking at the glucose molecule. Because (B), (C), and (D) have identical stereochemistry at C-4, they are incorrect.

59
Q

Andersen’s disease (glycogen storage disease type IV) is a condition characterized by a deficiency in glycogen branching enzyme. Absence of this enzyme would be likely to cause all of the following effects EXCEPT:
A. decreased glycogen solubility in human cells.
B. slower action of glycogen phosphorylase.
C. less storage of glucose in the body.
D. glycogen devoid of α-1,4 linkages.

A

D. glycogen devoid of α-1,4 linkages
In Andersen’s disease, glycogen is less branched than normal, thereby inducing lower solubility of glycogen.
Branches reduce the interactions between adjacent chains of glycogen and encourage interactions with the aqueous environment. The smaller number of branches means that glycogen phosphorylase has fewer terminal glucose monomers on which to act, making enzyme activity slower than normal overall. Finally, without branches, the density of glucose monomers cannot be as high; therefore, the total glucose stored is lower than normal. Glycogen synthase is still functioning normally, so we would expect normal a-1,4 linkages in the glycogen of an individual with Andersen’s disease but few if any) a-1,6 linkages.

60
Q

The cyclic forms of monosaccharides are:
I. hemiacetals.
Il. hemiketals.
Il. acetals.
A. I only
B. III only
C. I and II only
D. I, II, and III

A

C. I and II only

Monosaccharides can exist as hemiacetals or hemiketals, depending on whether they are aldoses or ketoses. When a monosaccharide is in its cyclic form, the anomeric carbon is attached to the oxygen in the ring and a hydroxyl group.
Hence, it is only a hemiacetal or hemiketal because an acetal or ketal would require the -OH group to be converted to another - OR group.

61
Q

Which of the following is NOT a type of glycolipid?
A. Cerebroside
B. Globoside
C. Ganglioside
D. Sphingomyelin

A

D. Sphingomyelin
Glycolipids contain sugar moieties connected to their back-bone. Sphingomyelin is not a glycolipid, but rather a phos-pholipid. This class can either have phosphatidylcholine or phosphatidylethanolamine as a head group and therefore contains a phosphodiester, not glycosidic, bond.

62
Q

During saponification:
A. triacylglycerols undergo a condensation reaction.
B. triacyglycerols undergo ester hydrolysis.
C. fatty acid salts are produced using a strong acid
D. fatty acid salts are bound to albumin.

A

B.

Saponification is the ester hydrolysis of triacylglycerol using a strong base like sodium or potassium hydroxide to form glycerol and fatty acid salts. This is not a condensation reac-tion, as in (A), but a cleavage reaction. Fatty acids do travel in the body bonded to serum albumin, as in (D), but that is unrelated to the process of saponification.

63
Q

Which of the following best describes the structure of steroids?
A. Three cyclopentane rings, one cyclohexane ring
B. Three cyclohexane rings, one cyclopentane ring
C. Four carbon rings, differing in structure for each steroid
D. Three cyclic carbon rings and a functional group

A

В. Three cyclohexane rings, one cyclopentane ring
The basic backbone of steroid structure contains three cyclohexane rings and one cyclopentane ring. Although the oxidation status of these rings varies for different steroids, the overall structure does not, as in (C).

64
Q

Soap bubbles form because fatty acid salts organize into:
A. lysosomes.
B. micelles.
C. phospholipid bilayers.
D. hydrogen bonds.

A

B. Micelles

Fatty acid salt micelles are responsible for the formation of soap bubbles. While phospholipids can form bilayers, as in (C), the fatty acids in soap are free fatty acids, not phospholipids.

65
Q

Steroid hormones are steroids that:
1. have specific high-affinity receptors.
Il. travel in the bloodstream from endocrine glands
to distant sites.
Ill. affect gene transcription by binding directly
to DNA.
A. I only
B. Ill only
C. I and II only
D. I and III only

A

C. I and II only

Steroid hormones are produced in endocrine glands and travel in the bloodstream to bind high-affinity receptors in the nucleus. The hormones receptor binds to DNA as part of the hormone-receptor complex, but the hormone itself does not.

66
Q

Why are tricylglycerols used in the human body for energy storage?

A. They are highly hydrated and therefore can store lots of energy
B. They always have short fatty acid chains for easy access by metabolic enzymes.
C. The carbon atoms of the fatty acid chains are highly reduced and therefore yield more energy upon oxidation.
D. Polysaccharides, which would actually be a better energy storage form, would dissolve in the body.

A

C. The carbon atoms of the fatty acid chains are highly reduced and therefore yield more energy upon oxidation.

Triacyglycerols are highly hydrophobic and therefore not highly hydrated (which would add extra weight from the water of hydration, taking away from the energy density of these molecules), eliminating (A). The fatty acid chains produce twice as much energy as polysaccharides during oxidation because they are highly reduced. The fatty acid chains vary in length and saturation.

67
Q

Which of the following is correct about fat-soluble
Vitamins?
I. Vitamin E is important for calcium regulation.
II. Vitamin D protects against cancer because it is a
biological antioxidant.
III. Vitamin K is necessary for the posttranslational introduction of calcium-binding sites.
IV. Vitamin A is metabolized to retinal, which is important for sight.

A. Ill only
B. I and II only
C. Ill and IV only
D. II, II, and IV only

A

C. III and IV only

Vitamin A is metabolized to retinal, which is important for sight. Vitamin D is metabolized to calcitriol, which is important for calcium regulation. Vitamin E is made up of tocopherols, which are biological antioxidants. Vitamin K is necessary for the introduction of calcium binding sites, such as during the posttranslational modification of pro-thrombin.

68
Q

Which of the following is true of amphipathic molecules?
A. They form protective spheres in any solvent, with hydrophobic molecules interior and hydrophilic
molecules exterior.
B. They have two fatty acid chains and a polar head group.
C. They are important to the formation of the phospholipid bilayer and soap bubbles.
D. They have a glycerol base.

A

C. They are important to the formation of the phospholipid bilayer and soap bubbles.

Phospholipids are amphipathic, as are fatty acid salts.
Although amphipathic molecules take spherical forms with hydrophobic molecules interior in aqueous solu-tion, as in (A), the opposite would be true in a nonpolar solvent. (B) describes phospholipids and sphingolipids, and (D) describes triacylglycerols and phospholipids; both groups do not include fatty acid salts.

69
Q

Which of the following is/are true about
sphingolipids?
I. They are all phospholipids.
II. They all contain a sphingosine backbone.
Ill. They can have either phosphodiester or glycosidic
linkages to their polar head groups.
A. I only
B. Ill only
c. II and III only
D. I, II, and III

A

B. III only
Sphingolipids can either have a phosphodiester bond, and therefore be phospholipids, or have a glycosidic linkage and therefore be glycolipids. Not all sphingolipids have a sphingosine backbone, as in statement II; some have related (sphingoid) compounds as backbones instead.

70
Q

Which of the following statements about saturation is FALSE?
A. It can describe the number of double or triple bonds in a fatty acid tail.
B. It determines at least one of the properties of membranes.
C. More saturated fatty acids make for a more fluid solution.
D. Fully saturated fatty acids have only single bonds.

A

C. More saturated fatty acids make for a more fluid solution.

More saturated fatty acids make for a less fluid solution.
This is because they can pack more tightly and form more noncovalent bonds, resulting in more energy being needed to disrupt the overall structure.

71
Q

Which of the following is true about glycerophospholipids?
A. Glycerophospholipids can sometimes be sphin-golipids, depending on the bonds in their head groups.
B. Glycerophospholipids are merely a subset of phospholipids.
C. Glycerophospholipids are used in the ABO blood typing system.
D. Glycerophospholipids have one glycerol, one polar head group, and one fatty acid tail.

A

В. Glycerophospholipids are merely a subset of phospholipids.
Glycerophospholipids are a subset of phospholipids, as are sphingomyelins. Glycerophospholipids are never sphingo-lipids because they contain a glycerol backbone (rather than sphingosine or a sphingoid backbone), eliminating (A).
Sphingolipids are used in the ABO blood typing system, eliminating (C). Glycerophospholipids have a polar head group, glycerol, and two fatty acid tails, not one, as in (D).

72
Q

Which of the following statements about terpenes
is FALSE?
A. Terpenes are strongly scented molecules that sometimes serve protective functions.
B. Terpenes are steroid precursors.
C. A triterpene is made of three isoprene moieties, and therefore has 15 carbons.
D. Terpenes are made by plants and insects.

A

C. A triterpene is made of three isoprene moieties, and therefore has 15 carbons.

A triterpene is made of six isoprene moieties (remember, one terpene unit contains two isoprene units), and therefore has a 30-carbon backbone.

73
Q

Which of the following is true about cholesterol?
A. Cholesterol always increases membrane fluidity in cells.
B. Cholesterol is a steroid hormone precursor.
C. Cholesterol is a precursor for vitamin A, which is produced in the skin.
D. Cholesterol interacts only with the hydrophobic tails of phospholipids.

A

B. Cholesterol is a steroid hormone precursor.

Cholesterol is a steroid hormone precursor that has variable effects on membrane fluidity depending on temperature, eliminating (A). It interacts with both the hydrophobic tails and the hydrophilic heads of membrane lipids, nullifying (D). It is also a precursor for vitamin D (not vitamin A), which can be produced in the skin in a UV-driven reaction, eliminating (C).

74
Q

Which of the following statements regarding prostaglandins is FALSE?
A. Prostaglandins regulate the synthesis of CAMP.
B. Prostaglandin synthesis is inhibited by NSAIDs.
C. Prostaglandins affect pain, inflammation, and smooth muscle function.
D. Prostaglandins are endocrine hormones, like steroid hormones.

A

D. Prostaglandins are endocrine hormones, like steroid hormones.

Prostaglandins are paracrine or autocrine signaling mol-ecules, not endocrine-they affect regions close to where they are produced, rather than affecting the entire body. Think of the swelling that happens when you bash your knee into your desk: your knee will swell, become discol-ored, and possibly bruise. Luckily, however, your entire body won’t swell as well.

75
Q

Which of the statements regarding waxes is FALSE?
A. Waxes generally have melting points above room temperature.
B. Waxes are produced only in plants and insects and therefore must be consumed by humans.
C. Waxes protect against dehydration and parasites.
D. Waxes are esters of long-chain fatty acids and long-chain alcohols.

A

B. Waxes are produced only in plants and insects and therefore must be consumed by humans.

Waxes are also produced in animals for similar protective functions, Cerumen, or earwax, is a prime example in humans.

76
Q

In a single strand of a nucleic acid, nucleotides are linked by:
A. Hydrogen bonds
B. Phosphodiester bonds
C. lonic bonds.
D. van der Waals forces.

A

B. Phosphodiester bonds

Nucleotides bond together to form polynucleotides. The 3’ hydroxyl group of one nucleotides sugar joins the 5’ hydroxyl group of the adjacent nucleotide’s sugar by a phos-phodiester bond. Hydrogen bonding, (A), is important for holding complementary strands together, but does not play a role in the bonds formed between adjacent nucleotides on a single strand.

77
Q

Which of the following statements regarding differences between DNA and RNA is FALSE?
A. In cells, DNA is double-stranded, whereas RNA is single-stranded.
B. DNA uses the nitrogenous base thymine; RNA uses uracil.
C. The sugar in DNA is deoxyribose; the sugar in RNA is ribose.
D. DNA strands replicate in a 5’ to 3’ direction, whereas RNA is synthesized in a 3’ to 5’ direction.

A

D. DNA strands replicate in a 5’ to 3’ direction, whereas RNA is synthesized in a 3’ to 5’ direction.

Because we are looking for the false statement, we have to read each choice to eliminate those that are true or find one that is overtly false. Let’s quickly review the main differences between DNA and RNA. In cells, DNA is double-stranded, with a deoxyribose sugar and the nitrogenous bases A, T, C, and G. RNA, on the other hand, is usually single-stranded, with a ribose sugar and the bases A, U, C, and G. (D) is false because both DNA replication and RNA synthesis proceed in a 5’ to 3’ direction.

78
Q

Which of the following DNA sequences would have the highest melting temperature?
A. CCAACCATCCG
B. CGCAATAATACA
C. CGTAATAATACA
D. CATAACAAATCA

A

A. CCAACCATCCG

The melting temperature of DNA is the temperature at which a DNA double helix separates into two single strands (denatures). To do this, the hydrogen bonds linking the base pairs must be broken. Cytosine binds to guanine with three hydrogen bonds, whereas adenine binds to thymine with two hydrogen bonds. The amount of heat needed to disrupt the bonding is proportional to the number of bonds. Thus, the higher the GC-content in a DNA segment, the higher the melting point.

79
Q

Which of the following biomolecules is LEAST likely to contain an aromatic ring?
A. Proteins
B. Purines
C. Carbohydrates
D. Pyrimidines

A

C. Carbohydrates
Aromatic rings must contain conjugated i electrons, which require alternating single and multiple bonds, or lone pairs.
In carbohydrate ring structures, only single bonds are present, thus preventing aromaticity. Nucleic acids contain aromatic heterocycles, while proteins will generally contain at least one aromatic amino acid (tryptophan, phenylala-nine, or tyrosine).

80
Q

For a compound to be aromatic, all of the following must be true EXCEPT:
A. the molecule is cyclic.
B. the molecule contains 4n + 2 m electrons.
C. the molecule contains alternating single and double bonds.
D. the molecule is planar.

A

C. the molecule contains alternating single and double bonds.

For a compound to be aromatic, it must be cyclic, planar, conjugated, and contain 4n + 2 i electrons, where n is any integer. Conjugation requires that every atom in the ring have at least one unhybridized p-orbital. While most examples of aromatic compounds have alternating single and double bonds, compounds can be aromatic if they contain triple bonds as well; this would still permit at least one unhybridized p-orbital.

81
Q

Which of the following enzymes is NOT involved in DNA replication?
A. Primase
B. DNA ligase
C. RNA polymerase I
D. Telomerase

A

С. RNA polymerase I
During DNA replication, the strands are separated by DNA helicase. At the replication fork, primase, (A), creates a primer for the initiation of replication, which is followed by DNA polymerase. On the lagging strand, Okazaki fragments form and are joined by DNA ligase, (B). After the chromosome has been processed, the ends, called telo-meres, are replicated with the assistance of the enzyme telo-merase, (D). RNA polymerase I is located in the nucleolus and synthesizes rRNA.

82
Q

How is DNA best characterized?
A. CDNA results from a DNA transcript with noncod. ing regions removed.
B. CDNA results from the reverse transcription of processed mRNA.
C. CDNA is the abbreviation for deoxycytosine.
D. CDNA is the circular DNA molecule that forms the bacterial genome.

A

B. CDNA results from the reverse transcription of processed mRNA.

CDNA (complementary DNA) is formed from a processed mRNA strand by reverse transcription. cDNA is used in
DNA libraries and contains only the exons of genes that are transcriptionally active in the sample tissue.

83
Q

Endonucleases are used for which of the following?
1. Gene therapy
II. Southern blotting
III. DNA repair
A. I only
B. Il only
C. Il and III only
D. I, II, and III

A

D. I, II, and III
Endonucleases are enzymes that cut DNA. They are used by the cell for DNA repair. They are also used by scientists during DNA analysis, as restriction enzymes are endonu-cleases. Restriction enzymes are used to cleave DNA before electrophoresis and Southern blotting, and to introduce a gene of interest into a viral vector for gene therapy.

84
Q

Which of the following statements regarding polymerase chain reaction is FALSE?
A. Human DNA polymerase is used because it is the most accurate.
B. A primer must be prepared with a complementary sequence to part of the DNA of interest.
C. Repeated heating and cooling cycles allow the enzymes to act specifically and replaces helicase.
D. Each cycle of the polymerase chain reaction doubles the amount of DNA of interest.

A

A. Human DNA polymerase is used because it is the most accurate.

The polymerase chain reaction is used to clone a sequence of DNA using a DNA sample, a primer, free nucleotides, and enzymes. The polymerase from Thermus aquaticus is used because the reaction is regulated by thermal cycling, which would denature human enzymes.

85
Q

How does prokaryotic DNA differ from
eukaryotic DNA?
I. Prokaryotic DNA lacks nucleosomes.
II. Eukaryotic DNA has telomeres.
IlI. Prokaryotic DNA is replicated by a different DNA
polymerase.
IV. Eukaryotic DNA is circular when not restricted by
centromeres.
A. I only
B. IV only
c. II and III only
D. I, Il, and III only

A

D. I, Il, and III only
Prokaryotic DNA is circular and lacks histone proteins, and thus does not form nudeosomes. Both prokaryotic and eukaryotic DNA are replicated by DNA polymerases, although these polymerases differ in identity. Eukaryotic DNA is organized into chromatin, which can condense to form linear chromosomes; only prokaryotes have circular chromosomes. Only eukaryotic DNA has telomeres.

86
Q

Why might uracil be excluded from DNA but NOT RNA?
A. Uracil is much more difficult to synthesize than thymine.
B. Uracil binds adenine too strongly for replication.
C. Cytosine degradation results in uracil.
D. Uracil is used as a DNA synthesis activator.

A

C. Cytosine degradation results in uracil.

One common DNA mutation is the transition from cytosine to uracil in the presence of heat. DNA repair enzymes recognize uracil and correct this error by excising the base and inserting cytosine. RNA exists only transiently in the cell, such that cytosine degradation is insignificant. Were uracil to be used in DNA under normal circumstances, it would be impossible to tell if a base should be uracil or if it is a damaged cytosine nucleotide.

87
Q

Tumor suppressor genes are most likely to result in cancer through:
A. loss of function mutations.
B. gain of function mutations.
C. overexpression.
D. proto-oncogene formation.

A

A. Loss of function mutations

Oncogenes are most likely to result in cancer through activation, (B), while tumor suppressor genes are most likely to result in cancer through inactivation.

88
Q

Which of the following is an ethical concern of gene sequencing?
A. Gene sequencing is invasive, thus the potential health risks must be thoroughly explained.
B. Gene sequencing impacts relatives, thus privacy concerns may be raised.
C. Gene sequencing is very inaccurate, which increases anxiety related to findings,
D. Gene sequencing can provide false-negative results, giving a false sense of security

A

B. Gene sequencing impacts relatives, thus privacy concerns may be raised.

One of the primary ethical concerns related to gene sequencing is the issue of consent and privacy. Because genetic screening provides information on direct relatives, there are potential violations of privacy in communicating this information to family members who may be at risk.
There are not significant physical risks, eliminating (A), and gene sequencing is fairly accurate, eliminating (C) and (D).

89
Q

Which of the following is NOT a difference between heterochromatin and euchromatin?
A. Euchromatin has areas that can be transcribed, whereas heterochromatin is silent.
B. Heterochromatin is tightly packed, whereas euchromatin is less dense.
C. Heterochromatin stains darkly, whereas euchro-matin stains lightly.
D. Heterochromatin is found in the nucleus, whereas euchromatin is in the cytoplasm.

A

D. Heterochromatin is found in the nucleus, whereas euchromatin is in the cytoplasm.

Euchromatin has a classic “beads on a string” appearance that stains lightly, while heterochromatin is tightly packed and stains darkly. Heterochromatin is primarily composed of inactive genes or untranslated regions, while euchromatin is able to be expressed. All chromatin is found in the nucleus, not the cytoplasm.

90
Q

During which phase of the cell cycle are DNA repair mechanisms least active?
A. G1
B. S
C. G2
D. M

A

D. M

Mismatch repair mechanisms are active during S phase (proofreading) and G2, phase (MSH2 and MLH1), eliminating (B) and (C). Nucleotide and base excision repair mechanisms are most active during the G1, and G2, phases, also eliminating (A). These mechanisms exist during interphase because they are aimed at preventing propagation of the error into daughter cells during M phase (mitosis).

91
Q

What role does peptidyl transferase play in protein synthesis?

A. It transports the initiator aminoacyl-tRNA complex.
B. It helps the ribosome to advance three nucleotides along the mRNA in the 5’ to 3’ direction.
C. It holds the protein in its tertiary structure.
D. It catalyzes the formation of a peptide bond

A

D. It catalyzes the formation of a peptide bond

Peptidyl transferase is an enzyme that catalyzes the formation of a peptide bond between the incoming amino acid in the A site and the growing polypeptide chain in the P site. Initiation and elongation factors help transport charged tRNA molecules into the ribosome and advance the ribosome down the mRNA transcript, as in (A) and (B). Chaperones maintain a protein’s three-dimensional shape as it is formed, as in (C).

92
Q

A mutation in which of the following components of the lac operon would lead to a significant reduction in the expression of lactase (one of the structural genes)?

A. Operator
B. Regulatory gene
C. Promoter
D. Structural genes

A

C. Promoter
The promoter functions as a recruitment site for RNA polymerase and is required for gene expression. A mutation in this region would hinder RNA polymerase recruitment, resulting in a decrease in gene expression. These observations support (C) as the correct answer. By contrast, mutations in the operator and regulatory genes would render the repressor less able to block transcription, leading to the opposite effect, i.e. an increase in lactase expression. This result eliminates both (A) and (B). Finally, mutations in the structural genes could lead to the production of a nonfunctional enzyme, but are unlikely to affect gene expression, eliminating (D).

93
Q

Topoisomerases are enzymes involved in:
A. DNA replication and transcription.
B. posttranscriptional processing.
C. RNA synthesis and translation.
D. posttranslational processing.

A

A. DNA replication and transcription.

Topoisomerases, such as prokaryotic DNA gyrase, are involved in DNA replication and mRNA synthesis (tran-scription). DNA gyrase is a type of topoisomerase that enhances the action of helicase enzymes by the introduc-ion of negative supercoils into the DNA molecule. These negative supercoils facilitate DNA replication by keeping the strands separated and untangled.

94
Q

Val-tRNAVal is the tRNA that carries valine to the ribosome during translation. Which of the following sequences gives an appropriate anticodon for this ERNA? (Note: Refer to Figure 7.5 for a genetic code table.)

A. CAU
B. AUC
C. UAC
D. GUG

A

C. UAC

There are four different codons for valine: GUU, GUC, GUA, and GUG. Through base-pairing, we can determine that the proper anticodon must end with “AC. Remember that the codon and anticodon are antiparallel to each other, and that nucleic acids are always written 5’ → 3’ on the MCAT. Therefore, we are looking for an answer that ends with “AC” (rather than starting with “CA”).

95
Q

Enhancers are transcriptional regulatory sequences that function by enhancing the activity of:
A. RNA polymerase at a single promoter site.
B. RNA polymerase at multiple promoter sites.
C. spliceosomes and lariat formation in the ribosome.
D. transcription factors that bind to the promoter but not to RNA polymerase.

A

A. RNA polymerase at a single promoter site

Specific transcription factors bind to a specific DNA sequence, such as an enhancer, and to RNA polymerase at a single promoter sequence. They enable the RNA polymerase to transcribe the specific gene for that enhancer more efficiently.

96
Q

In the genetic code of human nuclear DNA, one of the codons specifying the amino acid tyrosine is UAC. If one nucleotide is changed and the codon is mutated to UAG, what type of mutation will occur
A. Silent mutation
B. Missense mutation
C. Nonsense mutation
D. Frameshift mutation

A

C. Nonsense mutation

UAG is one of the three known stop codons, so changing tyrosine to a stop codon must be a nonsense (or truncation) mutation.

97
Q

Which of the following is NOT used by eukaryotes to increase the transcription of a gene?
A. Gene duplication
B. Histone acetylation
C. DNA methylation
D. Enhancers

A

C. DNA methylation

In this question, the correct answer is the answer that is not associated with increased transcription. DNA methylation, (C), is associated with silencing of gene expression. Regions of DNA with poor gene expression, called heterochromatin, are heavily methylated. These modifications significantly decrease the ability of RNA polymerase to access DNA.

98
Q

When trypsin converts chymotrypsinogen to chymotrypsin, some molecules of chymotrypsin bind to a repressor, which in turn binds to an operator region and prevents further transcription of trypsin. This is most similar to which of the following operons?
A. trp operon during lack of tryptophan
B. trp operon during abundance of tryptophan
C. lac operon during lack of lactose
D. lac operon during abundance of lactose

A

B. trp operon during abundance of tryptophan

The example given is a sample of repression due to the abundance of a corepressor. In other words, this is a repressible system that is currently blocking transcription.
For the trp operon, an abundance of tryptophan in the environment allows for the repressor to bind tryptophan and then to the operator site. This blocks transcription of the genes required to synthesize tryptophan within the cell.
The system described is a repressible system; the lac operon is an inducible system, in which an inducer binds to the repressor, thus permitting transcription.

99
Q

Which of the following RNA molecules or proteins is NOT found in the spliceosome during intron excision?
A. snRNA
B. hnRNA
C. shRNA
D. snRNPS

A

C. shRNA

shRNA (short hairpin RNA) is a useful biotechnology tool used in RNA interference. It is not, however, produced in the nucleus for use in the spliceosome. It targets mRNA to be degraded in the cytoplasm; it is not utilized in splicing of the nRNA (heterogeneous nuclear RNA). sRNA (small nuclear RNA) and snRNPs (small nuclear ribonucleopro-teins), however, do bind to the nRNA to induce splicing.

100
Q

A 4-year-old toddler with cystic fibrosis (CF) is seen by his physician for an upper respiratory infection.
Prior genetic testing has shown that there has been a deletion of three base pairs in exon 10 of the CFTR gene that affects codons 507 and 508.
The nucleotide sequence in this region for normal and mutant alleles is shown below X denotes the missing nucleotide):

What effect will this mutation have on the amino acid sequence of the protein encoded by the CFTR gene? (Note: Refer to Figure 7.5 for a genetic code table.)

A. Deletion of a phenylalanine residue with no change in the C-terminus sequence
B. Deletion of a leucine residue with no change in the C-terminus sequence
C. Deletion of a phenylalanine residue with a change in the C-terminus sequence
D. Deletion of a leucine residue with a change in the C-terminus sequence

A

A.

In this table, we are given the sequence of the sense (coding) DNA strand. This will be identical to the mRNA transcript, except all thymine nucleotides will be replaced with uracil. With the deletion of these three bases, codon 507 changes from AUC to AUU in the transcript; these both code for isoleucine due to wobble. However, codon 508 (UUU in the transcript) has been lost. UUU codes for phenylalanine. The C-terminus sequence will remain unchanged because the deletion of three bases (exactly one codon) will not throw off the reading frame. For reference, the mutant reading frames would be:
(Note: refer back to Figure 7.5 for a table of the genetic code)

101
Q

A gene encodes a protein with 150 amino acids.
There is one intron of 1000 base pairs (bp), a 5’-untranslated region of 100 bp, and a 3’-untranslated region of 200 bp. In the final mRNA, about how many bases lie between the start AUG codon and final termination codon?
A. 150
В. 450
С. 650
D. 1750

A

B. 450

The intron will not be a part of the final, processed mRNA, and the untranslated regions of the mRNA will not be turned into amino acids. Translation will begin with codon 1 (which would be AUG). Because there are 150 amino acids, we can surmise that there will be 151 codons. Each codon will use
3 nucleotides, so 150 x 3 = 450 because codon 151 will be
the stop codon.

102
Q

Peptidyl transferase connects the carboxylate group of one amino acid to the amino group of an incoming amino acid. What type of linkage is created in this peptide bond?
A. Ester
B. Amide
C. Anhydride
D. Ether

A

B. Amide

Peptidyl transferase connects the incoming amino terminal to the previous carboxyl terminal; the only functional group listed here with a carbonyl and amino group is the amide. Peptide bonds are thus amide linkages, and the correct answer is (B).

103
Q

A eukaryotic cell has been found to exhibit a truncation mutation that creates an inactive RNA polymerase I enzyme. Which type of RNA will be affected by this inactivation?
A. rRNA
B. tRNA
C. snRNA
D. hnRNA

A

A. rRNA
RNA polymerase I in eukaryotes is found in the nucleolus and is in charge of transcribing most of the RNA for use during ribosomal creation. RNA polymerase Il is responsible for hRNA and sRNA. RNA polymerase III is responsible for tRNA and the 5S rRNA.

104
Q

You have just sequenced a piece of DNA that reads as follows:

5’-TCTTTGAGACATCC-3’

What would the base sequence of the mRNA transcribed from this DNA be?

A. 5’—AGAAACUCUGUAGG—3’
B. 5’—GGAUGUCUCAAAGA-3’
C. 5’—AGAAACTCTGTAGG—3’
D. 5’-GGATCTCTCAAAGA-3’

A

B. 5’—GGAUGUCUCAAAGA-3’

To answer this question correctly, we must remember that mRNA will be antiparallel to DNA. Our answer should be 5’ to 3’ mRNA, with the 5’ end complementary to the 3’ end of the DNA that is being transcribed.
Thus, the mRNA transcribed from this strand will be 5’ -GGAUGUCUCAAAGA-3’. mRNA contains uracil, rather than thymine.

105
Q

Double-stranded RNA cannot be translated by the ribosome and is marked for degradation in the cell. Which of the following strands of RNA would prevent mature mRNA in the cytoplasm from being translated?
A. Identical mRNA to the one produced
B. Antisense mRNA to the one produced
C. mRNA with thymine substituted for uracil
D. Sense mRNA to the one produced

A

B. Antisense mRNA to the one produced

The mRNA produced has the same structure as the sense strand of DNA (with uracils instead of thymines).
Because bonding of nucleic acids is always complementary but antiparallel, the antisense strand of mRNA would be the one that binds to the produced mRNA, creating double-stranded RNA that is then degraded once found in the cytoplasm.