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
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.
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.
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
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.
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
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.
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.
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.
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
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).
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.
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.
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
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.
Which of the following is NOT involved in cell migration?
A. Dynein
B. Flagella
C. Actin
D. Centrioles
Which of the following proteins is most likely to be found extracellularly?
A. Tubulin
B. Myosin
C. Collagen
D. Actin
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
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.
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
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.
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.
Which of the following is NOT a component of all trimeric G proteins?
A. Gα
B. Gβ
C. Gγ
D. Gi
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.
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
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.
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
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.
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.
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.