Biochemistry Flashcards
In a neutral solution, most amino acids exist as:
A. positively charged compounds.
B. zwitterions.
C. negatively charged compounds.
D. hydrophobic molecules.
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.
At pH 7, the charge on a glutamic acid molecule IS:
A. -2.
B. -1.
C. 0.
D. +1.
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.
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
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.
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. 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.
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
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.)
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.
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).
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.
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.
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
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.
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
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.
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
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.
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.
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).
Which of these amino acids has a side chain that can become ionized in cells?
A. Histidine
B. Leucine
C. Proline
D. Threonine
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.
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.
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).
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
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.
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
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.
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.
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).
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. 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.
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.
B. Apoenzyme
An enzyme devoid of its necessary cofactor is called an apoenzyme and is catalytically inactive.
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. 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.
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
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.
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
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.
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. 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.
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
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).
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
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