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BCM 321 > Final Exam Review > Flashcards

Final Exam Review Flashcards

1
Q

High cellular concentrations of what molecule will inhibit the entry of pyruvate into the Kreb’s cycle?

a. AMP
b. NADH
c. Pyruvate
d. CoA

A

b. NADH

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2
Q

Where does the reactive oxygen species known as superoxide originate?

a. As a product of superoxide dismutase
b. From outside the body
c. As a naturally occurring by-product of body processes
d. As a malfunction of the ETC and oxidative phosphorylation

A

c. As a naturally occurring by-product of body processes

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3
Q

The phosphorylation of enzymes are catalyzed by protein…

a. Acetylases
b. Dephosphatases
c. Ligases
d. Kinases

A

d. Kinases

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4
Q

During which type of inhibition does a molecule structurally similar to the substrate bind to the active site?

a. Non-competitive
b. Competitive
c. Uncompetitive
d. Non-specific

A

b. Competitive

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5
Q

Which amino acid is most commonly found in protein structures?

a. L-amino acids
b. D-animo acids
c. Neither D nor L amino acids
d. R-configured amino acids

A

a. L-amino acids

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6
Q

What is the third amino acid in a collagen chain?

a. Valine
b. Isoleucine
c. Tryptophan
d. Glycine

A

d. Glycine

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7
Q

The glycoprotein Human erythropoietin is used therapeutically for anemia, what are the sugars likely attached to?

a. Proline and valine residues
b. Glycine and serine residues
c. Serine and asparagine residues
d. Histidine and cysteine residues

A

c. Serine and asparagine residues

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8
Q

Why do fatty acids usually contain an even number of carbon atoms?

a. All biological systems produce molecules with an even number of carbon atoms
b. Most fatty acids are synthesized in the ribosomes
c. Fatty acids are all the same length
d. Fatty acids are synthesized two carbons at a time

A

d. Fatty acids are synthesized two carbons at a time

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9
Q

At a pH of 12, what is (are) the charged group(s) present in a molecule of glycine?

a. -NH3+
b. -COO-
c. NH2+
d. NH3- and -COO-
e. All of the charged groups are present

A

b. -COO-

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10
Q

What type of binding is indicated by sigmoidal-shaped binding curve?

a. Competitive
b. Noncompetitive
c. Uncooperative
d. Cooperative
e. None of the above

A

d. Cooperative

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11
Q

What may happen within the cell if H+ ions were incapable of moving out of the mitochondrial matrix via Complexes I, III, and IV?

a. ATP production would halt.
b. Succinate would not be converted into Fumarate
c. The electron transport chain would cease to function.
d. ATP synthase would cease to function.
e. The inter-membrane space would increase in pH.

A

d. ATP synthase would cease to function.

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12
Q

If lipoic acid (involved in the transfer of an acetyl group from did not exist, what would happen?

a. Acetyl CoA would buildup in the cell.
b. Pyruvate would buildup in the cell
c. 1-6 bisphosphate would be further phosphorylated.
d. NADH will increase in concentration.
e. Fat metabolism will be increased.

A

e. Fat metabolism will be increased.

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13
Q

Which pathway yields 1 net ATP?

a. Pyruvate
b. Embden-Meyerhof
c. Entner-Doudoroff
d. Fermentation

A

c. Entner-Doudoroff

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14
Q

Which glycolytic intermediate participates in substrate level phosphorylation?

a. 1,3-bisphosphoglycerate
b. Fructose-1,6-bisphosphate
c. Glyceraldehyde-3-phosphate
d. Glucose-6-phosphate

A

a. 1,3-bisphosphoglycerate

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15
Q

Amino acids with what type of side chain are usually anchored in the plasma membrane in membrane bound proteins?

a. Small polar
b. Charged
c. Non-polar
d. Large polar

A

c. Non-polar

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16
Q

Why is rotation around a peptide bond restricted?

a. It has partial double bond character
b. R groups do not allow for rotation
c. Hydrogen bonding with carbonyl group and nitrogen
d. All bonds in a peptide are rotatable

A

a. It has partial double bond character

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17
Q

What is equal to the substrate concentration when the reaction is half its maximal value?

a. Kd
b. Vmax
c. Km
d. V0

A

c. Km

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18
Q

Catalysis occurs by which of the following?

a. Stabilizing the transition state.
b. Increasing the reactant reactivity.
c. Lowering the product concentration.
d. None of the above are correct.

A

a. Stabilizing the transition state.

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19
Q

What type of amino acid residues would be found in the interior of a cytosolic protein?

a. Polar
b. Charged
c. Hydrophobic
d. Hydrophilic
e. None of the above

A

c. Hydrophobic

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20
Q

When overlooking the BPG binding site in hemoglobin, how would you expect the BPG binding site to react like if you were to use a serine residue to replace the lysine residue?

a. The BPG site would tighten due to the loss of a positive charge in the lysine residue.
b. The BPG site will bind less tightly because the site replaced the positive charged lysine with a polar serine residue.
c. The BPG site would tighten due to the gain of a polar residue in serine.
d. The BPG site would bind less tightly because the site replaced the charged lysine with a polar serine.
e. The BPG site will have no reaction to the substitution of a lysine residue for a serine residue.

A

b. The BPG site will bind less tightly because the site replaced the positive charged lysine with a polar serine residue.

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21
Q

The use of a small amount of beta-marcaptoethanol on an already denatured protein does what?

a. Prevents formation of di-sulfide bonds
b. Prevents formation of hydrogen bonds
c. Further denatures the protein into separated amino acids
d. Promotes most energetically favorable formation of protein
e. Promotes quick renaturing of the protein

A

d. Promotes most energetically favorable formation of protein

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22
Q

Carbonic anhydrase has a significant impact on hemoglobin activity in what way?

a. Creates a more basic environment stabilizing hemoglobin R-state formation
b. Creates a more basic environment stabilizing hemoglobin T-state formation
c. Creates a more acidic environment stabilizing hemoglobin R-state formation
d. Creates a more acidic environment stabilizing hemoglobin T-state formation
e. None of the above

A

d. Creates a more acidic environment stabilizing hemoglobin T-state formation

23
Q
  1. What is physically bigger, a protein or the gene that codes for the protein?
    a. Depends if the protein has quaternary structure or not
    b. The gene because 3 amino acids result from 1 nucleotide
    c. The protein because an amino acid is bigger than a nucleotide
    d. The gene because 3 nucleotides code for 1 amino acid
A

d. The gene because 3 nucleotides code for 1 amino acid

24
Q

What functional group is present in all peptide bonds?

a. Thiol
b. Aldehyde
c. Amide
d. Carboxylic acid

A

c. Amide

25
Q

All of the following is true EXCEPT what?

a. Alanine can be converted to pyruvic acid via aminotransferase
b. Oxaloacetate can be converted from pyruvate via aminotransferase
c. Oxaloacetate can be converted from pyruvate via pyruvate carboxylase
d. Aspartic acid can be converted to oxaloacetate via aminotransferase

A

b. Oxaloacetate can be converted from pyruvate via aminotransferase

26
Q

What enzyme is responsible for connecting Glycolysis with the start of the Citric Acid Cycle (for harvesting further energy)?

a. Pyruvate Dehydrogenase
b. Alcohol Dehydrogenase
c. Pyruvate Reductase
d. Citric Synthase
e. Pyruvate Carboxylase

A

a. Pyruvate Dehydrogenase

27
Q

What is a product of the reaction catalyzed by Succinyl-CoA Synthase in the Citric Acid Cycle?

a. GTP
b. ADP
c. H20
d. FADH2
e. NAD+

A

a. GTP

28
Q

What are the direct products of repeated cycles of beta-oxidation starting with a fatty acid that is 9 carbons long?

a. 2 molecules of Acetyl-CoA and 2 molecules of Glycerol
b. 3 molecules of Glyceraldehyde-3-phosphate
c. 4 molecules of Acetyl CoA and one Methane
d. 3 molecules of Acetyl CoA and one molecule of Propionyl-CoA
e. 9 molecules of Acetyl-CoA

A

d. 3 molecules of Acetyl CoA and one molecule of Propionyl-CoA

29
Q

What is the first step taken towards breakdown of stored triglycerides?

a. Feedforward Stimulation of Trigylceride Lipase
b. Oxidation of bond between beta and alpha carbon
c. Inactivation of Perilipin
d. Hydration of beta carbon
e. Addition of CoA to Fatty Acids

A

c. Inactivation of Perilipin

30
Q

Which of the following conditions would you predict to lead to an increase in free radical production by NADH dehydrogenase (complex I)?

a. Large amounts of NADH and/or ubiquinol (QH2)
b. Iron deficiency
c. Low levels of ATP
d. Hypoxia
e. Low levels of FAD+

A

a. Large amounts of NADH and/or ubiquinol (QH2)

31
Q

By which mechanism do protons transverse the F0 ring of ATP Synthase?

a. Interactions with Iron-Sulfur clusters
b. Transfer through Glycerol-3-phosphate shuttle
c. Freely moving through a pore large enough to accommodate protons
d. Protonation of an Aspartic Acid residue on a C subunit
e. Reduction of FAD to form FADH2

A

d. Protonation of an Aspartic Acid residue on a C subunit

32
Q

Which of the following is the normal electron donor for the reaction catalyzed by Cytochrome c reductase?

a. Cytochrome C
b. Ubiquinone (Q)
c. FADH2
d. Ubiquinol (QH2)
e. Oxygen Gas

A

d. Ubiquinol (QH2)

33
Q

The Randle Cycle describes the reciprocal regulation between Glycolysis and Beta-oxidation. At what molecule do these pathways intersect?

A

Glycolysis and Beta-oxidation intersect at Acetyl CoA.

34
Q

What is the purpose, if any, of the uncoupling promoted like H+ transport proteins like UCP-1?

A

Produce heat

35
Q

Which of the following enzymatic regulation strategies is likely to enable the quickest response to the change in concentration for a small molecule?

a. Opening voltage gated ion channel to activate a protein kinase
b. Ubiquination and degradation of the enzyme
c. Direct allosteric regulation of the enzyme
d. Activation of transcription for the enzyme’s gene

A

c. Direct allosteric regulation of the enzyme

36
Q

What advantage(s) does allosteric regulation of an enzyme offer over a similar regulation by a competitive inhibitor?

A

The kinetics display an altered sigmodial curve, allowing a switch or toggle like behavior by the enzyme across a particular threshold of substrate

37
Q

What are all of the ways in which isozymes might be expected to differ?

A
  1. Presence or types of allosteric sites
  2. Km values for the same substrate

Types of bonds, reaction mechanisms, and products do NOT differ between isozymes

38
Q

Which of the following amino acids would you be most likely to encounter in a transmembrane helix?

a. Glutamate
b. Alanine
c. Serine
d. Lysine

A

b. Alanine

39
Q

What best describes the difference between Glucose and Fructose?

a. The number of carbon atoms
b. One is a monosaccharide, the other is a disaccharide
c. One is polar, the other is nonpolar
d. The position of the carbonyl group within the structure

A

d. The position of the carbonyl group within the structure

40
Q

What mutation can you introduce that would mimic permanent phosphorylation in a protein?

a. Substitution with Threonine
b. Substitution with Alanine
c. Substitution with Aspartate or Glutamate
d. Substitution with Asparagine or Arginine

A

c. Substitution with Aspartate or Glutamate

41
Q

What methods can be used to determine the amino acid sequence of a polypeptide?

A
  1. Edman degradation

2. Mass spectrometry

42
Q

Which of the following explains why myoglobin does not exhibit cooperative binding of oxygen?

a. Myoglobin does not change its conformation when oxygen binds.
b. Myoglobin has multiple oxygen binding sites.
c. Myoglobin does not bind oxygen, hemoglobin does.
d. Myoglobin only has one oxygen binding site.

A

d. Myoglobin only has one oxygen binding site.

43
Q

What are all the ways which stabilize hemoglobin in the T state?

A
  1. CO2
  2. Low pH
  3. 2,3-Bisphosphoglycerate
44
Q

Which amino acid is bound to the iron atom in heme?

A

Histidine

45
Q

Which of the following explains why restriction enzymes are a useful tool for biochemists?

a. They hydrolyze phosphodiester bonds randomly throughout a nucleic acid polymer.
b. They hydrolyze peptide bonds at specific amino acid sequences in a polypeptide.
c. They hydrolyze phosphodiester bonds at specific nucleotide sequences in a nucleic acid polymer.
d. They hydrolyze peptide bonds randomly throughout a polypeptide.

A

c. They hydrolyze phosphodiester bonds at specific nucleotide sequences in a nucleic acid polymer.

46
Q

The cooperative binding mechanism of hemoglobin is significant because…

a. It maximizes the fractional saturation of hemoglobin in the presence of CO2
b. It maximizes the fractional saturation of hemoglobin in the presence of 2,3-BPG
c. It maximizes the difference in fractional saturation of hemoglobin between tissues that are at rest and tissues that are active
d. It minimizes the difference in fractional saturation of hemoglobin between tissues that are at rest and tissues that are active

A

c. It maximizes the difference in fractional saturation of hemoglobin between tissues that are at rest and tissues that are active

47
Q

Hemoglobin has a higher affinity for oxygen at pH 7.4 than at pH 7.2. Which amino acid is responsible for the sensitivity of hemoglobin to such a subtle change in pH?

A

Histidine

48
Q

Delta G (free energy change) of a reaction depends on which of the following?

a. reaction rate
b. catalytic mechanism
c. concentration of reactants and products
d. number of steps in the pathway

A

c. concentration of reactants and products

49
Q

Which of the following describes the role of an enzyme?

a. make a non-spontaneous reaction into a spontaneous reaction
b. increase the delta G of the reaction
c. decrease the delta G of the reaction
d. increase the rate of the reaction

A

d. increase the rate of the reaction

50
Q

What are the reasons why RNA can perform a wide range of functions?

A
  1. RNA is single stranded
  2. Different RNA molecules may form different shapes or conformations
  3. RNA may form intramolecular complementary base pairs
51
Q

What did Watson and Crick suggest was significant about their hypothesized double helix structure of DNA?

A

The double helix structure suggested a mechanism for self-replication.

52
Q

What happens to hydrophobic molecules in water?

A

They come together excluding water molecules from their surfaces.

53
Q

What is the [A–]/[HA] ratio when a weak acid is in a solution one pH unit below its pKa?

A

1/10

BCM 321 (2 decks)

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