Biochemistry Flashcards

(168 cards)

1
Q

Glucose and fructose are examples of
double sugars
disaccharides
single sugars
polysaccharides

A

single sugars

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2
Q

(CH2O)n is the molecular formula for
which type of macromolecules?
Proteins
Lipids
Carbohydrates
Nucleic Acid

A

Carbohydrates

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3
Q

Which of the following is NOT a
polysaccharide?
Glycogen
Starch
Sucrose
Cellulose

A

Sucrose

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4
Q

What are used in animals as a source of
quick energy that can be stored in the
liver and muscles ?
Proteins
Nucleic acids
Carbohydrates
Lipids

A

Carbohydrates

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5
Q

Sugars, starches, and cellulose belong to which major class of biological molecules?
Nucleic acids
carbohydrates
lipids
polypeptides

A

carbohydrates

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6
Q

Plants like sugar cane and sugar beets store
the energy as simple sugars. Other plants,
like corn and potatoes, store the energy as
more complex sugars called?
carbohydrates
calories
starches
cellulose

A

starches

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7
Q

Which macromolecule does not
dissolve in water?
proteins
lipids
carbohydrates
nucleic acids

A

lipids

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8
Q

Monosaccharides have yellow appearance and are soluble in water. True or False?
True, they are yellow and soluble in water.
False, they are yellow and are insoluble in
water
False, they are colorless and are soluble in
water
False, they are colorless and insoluble in
water.

A

False, they are colorless and are soluble in water

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9
Q

What are the monomers of lipids?
Amino acids
Simple sugars
Fatty acids and glycerol
Nucleic acids

A

Fatty acids and glycerol

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10
Q

Lipids are used by the body to perform all
of the following functions EXCEPT:
membrane structural material.
enzyme action.
insulation.
a rich energy source.

A

enzyme action.

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11
Q

What type of organic substances are fats?
nucleic acid
carbohydrate
protein
lipids

A

lipids

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12
Q

Fats that have fatty acids with only single
covalent bonds in their carbon skeletons
are
saturated
unsaturated
found in plants instead of animals
liquid at room temperature

A

saturated

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13
Q

Which has the higher melting point: (a) a
triglyceride containing only lauric acid and
glycerol or (b) a triglyceride containing
only stearic acid and glycerol?
(a)
(b)
Both have equal melting points
None of the above

A

(b)

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14
Q

Which of the following is a polymer?
nucleic acid
fatty acid
Amino acid
Glycerol

A

nucleic acid

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15
Q

This biological macromolecule is
responsible for controlling the activity of the
cell, and it stores and transports genetic
information.
Carbohydrate
Nucleic acid
Water
Glucose

A

Nucleic acid

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16
Q

What are described as the “building
blocks of Protein”?
Fiber
Lipids
Amino Acids
Nutrients

A

Amino Acids

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17
Q

Proteins are ____ made of ____ amino acid .
monomers; polymers
polymers; polypeptides
polymers; monomers
monomers; molecules

A

polymers; monomers

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18
Q

In this type of structure, most of carbonyl
groups of peptide bonds forms a hydrogen
bond with the amide nitrogen of another
peptide bond four amino acids further down
the polypeptide chain:
Alpha-helix
Beta-sheet
Beta-turn
Quaternary

A

Alpha-helix

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19
Q

The isoelectric point of an amino acid is defined as the pH
where the molecule carries no electric charge
where the carboxyl group is uncharged
where the amino group is uncharged
of maximum electrolytic mobility

A

where the molecule carries no electric charge

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20
Q

When the amino acid alanine (R-group is CH3) is added to a solution with a pH of 7.3, alanine becomes
a cation
nonpolar
a zwitterions
an anion

Isoelectric point of alanine is 6.00

A

an anion

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21
Q

The term “SALTING IN” refers to?
Changes in an amino acid’s isoelectric
point.
Increasing the solubility of a protein in
solution by adding ions.
The use of a liquid bridge in an
electrochemical cell.
The ionization of a strong acid.

A

Increasing the solubility of a protein in solution by adding ions.

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22
Q

The local spatial arrangement of a
polypeptide’s backbone atoms without regard
to the conformation of its side chains can be
called as
Primary structure
Secondary structure
Tertiary structure
Quaternary structure

A

Secondary structure

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23
Q

Which of the following amino acids are
more likely to be found in a protein’s
interior away from aqueous solvent
molecules?
Val, Leu, Ile, Met, and Phe
Ser, Thr, Asn, Gln, and Tyr
Arg, His, Lys, Asp, and Glu
All of the above.

A

Val, Leu, Ile, Met, and Phe

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24
Q

Which of the following is (are) true of β- turns in proteins?
It is a 180º turn of four amino acids.
Glycine and proline are frequently found there.
Are used as connecting turns of -helix
All of the above.

A

All of the above.

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25
The primary stabilizing force of protein secondary structure is: Ionic bonds. Covalent bonds. Van der Waals forces. Hydrogen bonds
Hydrogen bonds
26
Two types of β-pleated sheets can be called: parallel and antiparallel left-handed and right-handed. Φ and Ψ α and β
parallel and antiparallel
27
Which of the following is NOT a characteristic of a globular protein? Polypeptide chain in extended, long sheets Polypeptide chains are folded in a spherical shape. Contains several types of secondary structure Typical for regulatory proteins
Polypeptide chain in extended, long sheets
28
The alpha helix found in myoglobin can best be described as Primary structure Secondary structure Tertiary structure Motif structure
Secondary structure
29
Some parts of a protein that have a specific chemical structure and function are called protein chemicals domains subunits enzymes
domains
30
One of the following is NOT usually a force that helps to hold the monomer units of a quaternary protein together? Peptide bonds Disulfide bonds Salt bonds Hydrophobic interactions
Peptide bonds
31
Which of the following is a secondary structure breaker/alpha helix terminator? Pro Glu, Leu Phe Cys, Ser
Pro
32
If a person breathes into a paper bag, you would expect their blood CO2 to decrease and their blood pH to increase decrease and their blood pH to decrease increase and their blood pH to increase increase and their blood pH to decrease
increase and their blood pH to decrease
33
The quaternary structure of a protein is the sequence of amino acids in the polypeptide the coiling or folding of the polypeptide the intertwining of two or more polypeptides the 3-dimensional appearance of the polypeptide
the intertwining of two or more polypeptides
34
The action of disrupting the threedimensional shape of a protein is termed dehydration denaturation deamination hydrolysis
denaturation
35
At a pH > pI of a given protein, that protein becomes ____, at the pH < pI of that same protein, it becomes ____.
negatively charged (an anion), positively charged (a cation)
36
The amino acid found in protein structure Arginine Proline Histidine Lysin
Arginine
37
The bonds in protein structure that are not broken on denaturation. Hydrogen bonds Peptide bonds lonic bond Disulfide bonds
Peptide bonds
38
What is the product of the oxidation of dopamine R-Epinephrine Phenylalanine Tyrosine Dihydroxyphenylalanine
R-Epinephrine
39
Which of the following is not considered a pyrimidine? C T U G
G ## Footnote PYCUT - Pyramidine ~ Cytosine Uracil Thymine PURGA - Purine ~ Adenine Guanine
40
What type of sugar is found in the nucleotides of DNA? deoxyribose ribose glucose none of the above
deoxyribose
41
What is the role of hydrogen bonds in the structure if DNA? to code for proteins to synthesize proteins to separate the strands to connect the base pairs
to connect the base pairs
42
Nucleoside is a pyrimidine or purine base covalently bonded to a sugar ionically bonded to a sugar hydrogen bonded to a sugar none of the above
covalently bonded to a sugar
43
The sugar in RNA is ____ , the sugar in DNA is ____ deoxyribose, ribose ribose, deoxyribose ribose, phosphate ribose, uracil
ribose, deoxyribose
44
In gel electrophoresis, what fragments will move most quickly through a gel? Large fragments Small fragments Large genome None of these
Small fragments
45
Nucleotide bases and aromatic amino acids absorb light respectively at 280 and 260 nm 260 and 280 nm 270 and 280 nm 260 and 270 nm
260 and 280 nm
46
Which of the following is found on RNA but not DNA? Uracil Deoxyribose Phosphate Adenine
Uracil ## Footnote DNA - CAGT = Cytosine, Adenine, Guanine, Thymine RNA - CAGU = Cytosine, Adenine, Guanine, Uracil
47
Which is true about the pairing of bases in the DNA molecule? purines always pair with pyrimidines a single ring base pairs with another single ring base a double ring base pairs with another double ring base purines pair with purines and pyrimidines with pyrimidines
purines always pair with pyrimidines
48
A messenger acid is 336 nucleotides long, including the initiator and termination codons. The maximum number of amino acids in the protein translated from this mRNA is: 999 630 330 111 110
111 ## Footnote start: AUG - methionine AGC - serine AGG - arginine GUC - valine (336 - 3) (1/3) = 111
49
What is the function of enzymes within living systems? structural elements neurotransmitters catalysts hormones
catalysts
50
Enzymes have names that always end in -ase always end in -in can end either in -in or -ase can end in either -in or -ogen
can end either in -in or -ase
51
The protein portion of a conjugated enzyme is called a(n) apoenzyme. coenzyme. holoenzyme. cofactor.
apoenzyme. ## Footnote apoenzyme - protein portion
52
Which of the following could be a component of a conjugated enzyme? coenzyme cofactor apoenzyme more than one correct response no correct response
more than one correct response
53
Enzyme cofactors that bind covalently at the active site of an enzyme are referred to as . cosubstrates. prosthetic groups. apoenzymes. vitamins
prosthetic groups.
54
Which of the following statements concerning the effect of temperature change on an enzyme-catalyzed reaction is correct? An increase in temperature can stop the reaction by denaturing the enzyme. An increase in temperature can increase the reaction rate by increasing the speed at which molecules move. An increase in temperature to the optimum temperature maximizes reaction rate. more than one correct response no correct response
more than one correct response
55
A catalyst can promote product formation during a chemical reaction by lowering the activation energy barrier. stabilizing the transition state. positioning reactants in the correct orientation. bringing reactants together. all of the above
all of the above
56
Which of the following is characteristic of an enzyme catalyst? It positions reactants in the correct orientation. It lowers the activation energy barrier. It binds the transition state tighter than the substrate. all of the above
all of the above
57
An enzyme active site is the location in the enzyme where protein side groups are brought together by bending and folding to form a site for interactions with substrates the catalyst interactions with the enzyme catalyst molecules are generated the substrate creates the catalyst molecules
protein side groups are brought together by bending and folding to form a site for interactions with substrates
58
An enzyme active site is the location in an enzyme where substrate molecules are generated. become catalysts. undergo change. none of these
undergo change.
59
For the enzyme reaction A+ B = C + D, Delta Go' = + 1 kcal/mol. This reaction will proceed spontaneously in a forward direction if: The concentration of C is increased one-hundred fold The concentration of A is increased one-hundred fold The concentration of B is lowered one-hundred fold The concentration of both A and D are increased onehundred fo
The concentration of A is increased one-hundred fold
60
Which of the following statements about enzymes or their function is true? Enzymes do not alter the overall change in free energy for a reaction Enzymes are proteins whose three-dimensional form is key to their function Enzymes speed up reactions by lowering activation energy All of the above
All of the above
61
What is the optimal temperature range for the majority of enzymes? 40-55 ℃ 35-40 ℃ 25-30 ℃ 15-20 ℃
35-40 ℃
62
An allosteric activator increases the binding affinity decreases the binding affinity stabilizes the R state of the protein both (a) and (c)
both (a) and (c)
63
Reactants of an enzyme-catalyzed reaction are known as products substrates proteins complex
substrates
64
The location on an enzyme where binding occurs is known as the action point enzyme binding location active site
active site
65
Enzymes catalyze reactions by Increasing the free energy of the system so that the change in free energy is positive Increasing the free energy of the substrate so that it isgreater than the free energy of the product Changing the equilibrium constant for the reaction Decreasing the free energy of activation
Decreasing the free energy of activation
66
An apoenzyme Includes non-protein compounds such as metal ions Consists of complex organic structures which may be classified as activation-transfer coenzymes or oxidationreduction coenzymes Is the protein portion of the enzyme without the cofactors None of the above
Is the protein portion of the enzyme without the cofactors ## Footnote apoenzyme - protein portion
67
NAD+, FAD, and FMN are all cofactors for: Oxidoreductases Transferases Hydrolases Ligases
Oxidoreductases
68
At the end of a chemical reaction an enzyme's structure is altered an enzyme is detached from the product, has its original structure, and can catalyzemore chemical reactions the enzyme loses its ablity to catallyze other chemical reactions the enzyme remains attached to the products
an enzyme is detached from the product, has its original structure, and can catalyze more chemical reactions
69
The rate of a second order reaction depends on the concentration of ____. one substrate two substrates three substrates none of the above
two substrates
70
Which of the following statements about allosteric enzymes is CORRECT? The binding of substrate to any active site affects the other active sites The plot of initial velocity vs. substrate concentration is a straight line The Keq of the reaction is increased when allosteric activator is bound The enzymes contains only one polypeptide chain
The binding of substrate to any active site affects the other active sites
71
Which of the following kinetic parameters best describes how well suited a specific compound functions as a substrate for a particular enzyme? Km Vmax kcat kcat/Km
kcat/Km ## Footnote Km - substrate specificity; substrate binding kcat - turnover number kcat/Km - catalytic efficiency
72
The rate-determining step of Michaelis Menten kinetics is the complex formation step the complex dissociation step to produce product the product formation step Both (a)and(c)
the complex dissociation step to produce product
73
A competitive inhibitor of an enzyme works by fitting into the enzyme's active site fitting into the allosteric site of the enzyme attaching itself to the substrate, thereby preventing the enzyme from making contact with substrate increasing the activation energy of the enzymecatalyzed reaction
fitting into the enzyme's active site
74
If an enzyme is described by the Michaelis-Menten equation, a competitive inhibitor will: decrease the Km and decrease the Vmax decrease the Km, but not the Vmax always just change the Vmax increase the Km but not change the Vmax
increase the Km but not change the Vmax
75
The most likely effect of a non-competitive inhibitor on an Michaelis-Menten enzyme is to Increase the Vmax Decrease the Vmax Increase both the Vmax and the Km Decrease both the Vmax and the Km
Decrease the Vmax
76
Which of the following binds to an enzyme at its active site? irreversible inhibitor reversible competitive inhibitor reversible noncompetitive inhibitor more than one correct response no correct response
reversible competitive inhibitor
77
An uncompetitive inhibitor binds to ____. E ES P a and b
ES
78
A reversible inhibitor that can bind to either E alone or the ES complex is referred to as a . competitive inhibitor. non-competitive inhibitor. uncompetitive inhibitor. suicide inhibitor. irreversible inhibitor.
non-competitive inhibitor
79
A competitive inhibitor of an enzyme is usually a highly reactive compound a metal ion such as Hg2+or Pb2+ structurally similar to the substrate. water insoluble
structurally similar to the substrate.
80
The enzyme inhibition can occur by reversible inhibitors irreversible inhibitors Both (a) and (b) None of these
Both (a) and (b)
81
In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect? It moves the entire curve to right It moves the entire curve to left It changes the x-intercept It has no effect on the slope
It changes the x-intercept
82
Non-competitive inhibitor of an enzyme catalyzed reaction decreases Vmax binds to ES both (a) and (b) can actually increase reaction velocity in rare cases
both (a) and (b)
83
A classical uncompetitive inhibitor is a compound that binds reversibly to the enzyme substrate complex yielding an inactive ESI complex irreversibly to the enzyme substrate complex yielding an inactive ESI complex reversibly to the enzyme substrate complex yielding an active ESI complex irreversibly to the enzyme substrate complex yielding an active ESI complex
reversibly to the enzyme substrate complex yielding an inactive ESI complex
84
Allosteric modulators seldom resemble the substrate or product of the enzyme. What does this observation show? Modulators likely bind at a site other than the active site. Modulators always act as activators. Modulators bind non-covalently to the enzyme. The enzyme catalyzes more than one reaction
Modulators likely bind at a site other than the active site.
85
Some enzymatic regulation is allosteric. In such cases, which of the following would usually be found? cooperativity feedback inhibition both activating and inhibitory activity an enzyme with more than one subunit the need for cofactors
an enzyme with more than one subunit
86
How many moles of lactate are produced from 3 moles of glucose 2 4 6 8
6
87
Glycolytic pathway regulation involves allosteric stimulation by ADP allosteric inhibition by ATP feedback, or product, inhibition by ATP all of the above
feedback, or product, inhibition by ATP
88
Why does the glycolytic pathway continue in the direction of glucose catabolism? There are essentially three irreversible reactions that act as the driving force for the pathway High levels of ATP keep the pathway going in a forwarddirection The enzymes of glycolysis only function in one direction Glycolysis occurs in either direction
There are essentially three irreversible reactions that act as the driving force for the pathway
89
The released energy obtained by oxidation of glucose is stored as a concentration gradient across a membrane ADP ATP NAD+
ATP
90
For every one molecule of sugar glucose which is oxidized molecule of pyruvic acid are produced. 1 2 3 4
2
91
The enzymes of glycolysis in a eukaryotic cell are located in the intermembrane space plasma membrane cytosol mitochondrial matrix
cytosol
92
Which of the following is not true of glycolysis? ADP is phosphorylated to ATP via substrate level phosphorylation The pathway does not require oxygen The pathway oxidizes two moles of NADH to NAD+for each mole of glucose that enters The pathway requires two moles of ATP to get startedcatabolizing each mole of glucose
The pathway oxidizes two moles of NADH to NAD+for each mole of glucose that enters
93
ATP is from which general category of molecules? Polysaccharides Proteins Nucleotides Amino acids
Nucleotides
94
Which of the following regulates glycolysis steps? Phosphofructokinase Hexose kinase Pyruvate kinase All of these
All of these
95
Which of the following is not a mechanism for altering the flux of metabolites through the rate-determining step of a pathway? Allosteric control of the enzyme activity Block active sites Genetic control of the enzyme concentration Covalent modification of the enzyme
Block active sites
96
Phosphofructokinase, the major flux-controlling enzyme of glycolysis is allosterically inhibited and activated respectively by ATP and PEP AMP and Pi ATP and ADP Citrate and ATP
ATP and ADP
97
Where does glycolysis occur? inner membrane of mitochondria matrix of mitochondria stroma of chloroplast cytoplasm
cytoplasm
98
Sports physiologists wanted to monitor athletes to determine at what point their muscles were functioning anaerobically. They could do this by checking for a buildup of which of the following compounds? oxygen ATP lactate carbon dioxide
lactate
99
There are four enzymes of gluconeogenesis that circumvent the irreversible steps in glycolysis. When starting with the substrate pyruvate or lactate they are Hexokinase, phosphofructokinase-1, phosphofructokinase-2 and pyruvate kinase Pyruvate carboxylase, phosphoenolpyruvate carboxykinase, fructose-1,6-bisphosphatase, and glucose-6-phosphatase Glycerol kinase, glycerol-3-phosphate dehydrogenase, fructose-2,6-bisphosphatase, and glucose-6-phosphatase Amino transferase, phosphoenolpyruvate carboxykinase, fructose-2,6-bisphosphatase, and glucose-6-phosphatase
Pyruvate carboxylase, phosphoenolpyruvate carboxykinase, fructose-1,6-bisphosphatase, and glucose-6-phosphatase
100
The enzymes that remove phosphate groups during the process of gluconeogenesis and circumvent two of the three irreversible reactions of glycolysis are Pyruvate kinase and glycerol kinase Phosphoenolpyruvate carboxykinase and glycerol kinase 3-Phosphoglycerate kinase and fructose-1,6-bisphosphatase Fructose-1,6-bisphosphatase and glucose-6-phosphatase
Fructose-1,6-bisphosphatase and glucose-6-phosphatase
101
The most important control step in gluconeogenesis is fructose-1,6- bisphosphatase. All of the following statements are true EXCEPT Fructose-1,6-bisphosphatase converts fructose-2,6-bisphosphate to fructose-6-phosphate During times when insulin is high, fructose-1,6-bisphosphatase is inhibited by fructose-2,6-bisphosphate During a fast or exercise when glucagon and/or epinephrine are high, fructose-1,6-bisphosphatase is active because of the absence of fructose-2,6-bisphosphate Glycolysis or gluconeogenesis cannot be active at the same time. If they were is would be a futile cycle
Fructose-1,6-bisphosphatase converts fructose-2,6-bisphosphate to fructose-6-phosphate
102
In the liver, glucagon will activate Glycolysis and glycogen synthesis Gluconeogenesis and glycogenolysis Gluconeogenesis and glycogen synthase Gluconeogenesis and glycogen synthesis
Gluconeogenesis and glycogenolysis
103
Which of the following statements about hormonal levels during different states is true? During the time you are eating a high carbohydrate mixed meal, the insulin to glucagon ratio will decrease When passing from the fed to fasting state, insulin and glucagon usually decrease When playing basketball, epinephrine is usually low and insulin is high After running for 20 miles, epinephrine and glucagon are high and insulin is low
After running for 20 miles, epinephrine and glucagon are high and insulin is low
104
All of the following will result in activation ofglycogen phosphorylase in skeletal muscle EXCEPT Increased concentrations of AMP from contraction of muscle Increased epinephrine and cAMP Increased cytosolic [Ca++] Increased protein phosphatase Increased activity of glycogen phosphorylase kinase
Increased protein phosphatase
105
A biological redox reaction always involves an oxidizing agent a gain of electrons a reducing agent all of these
all of these
106
Coenzyme Q is involved in electron transport as directly to O2 a water-soluble electron donor covalently attached cytochrome cofactor a lipid-soluble electron carrier
a lipid-soluble electron carrier
107
FAD is reduced to FADH2 during electron transport phosphorylation lactate fermentation Krebs cycle glycolysis
Krebs cycle
108
During glycolysis, electrons removed from glucose are passed to FAD NAD+ acetyl CoA pyruvic acid
NAD+
109
Almost all of the oxygen (O2) one consumes in breathing is converted to: acetyl-CoA. carbon dioxide (CO2). carbon monoxide and then to carbon dioxide. water.
water
110
The carbon dioxide is primary a product of Krebs cycle glycolysis electron transport phosphorylation. lactate fermentation.
Krebs cycle
111
Cellular respiration takes place mostly in: chloroplasts ribosomes nucleus mitochondria
mitochondria
112
Which of the following is not present during the TCA cycle? NADH O2 CO2 ATP
O2
113
Which of the following is a list of the stages in the correct order? pyruvate oxidation, glyocolysis, the citric acid cycle, and oxidative phosphorylation oxidative phosphorylation, glyocolysis, the citric acid cycle, and pyruvate oxidation glycolysis, pyruvate oxidation, the citric acid cycle, and oxidative phosphorylation glycolysis, the citric acid cycle, pyruvate oxidation, and oxidative phosphorylation
glycolysis, pyruvate oxidation, the citric acid cycle, and oxidative phosphorylation
114
What are the products of the citric acid cycle? NADH, ATP, FADH2, and CO2 O2, ADP, 1 FAD, and NAD+ Glucose, ATP, O2, and NADH heat, H2O, NADH, and pyruvate
NADH, ATP, FADH2, and CO2
115
Which of the following is NOT a way of producing ATP in humans? Krebs Cycle Alcohol Fermentation Lactic Acid Fermentation Glycolysis
Alcohol Fermentation
116
Which of the following is an aerobic product of pyruvate catabolic metabolism? lactate ethanol acetyl CoA glucose
ethanol
117
The TCA cycle: Is found in the cytosol Is controlled by the ADP/ATP ratio and the NADH concentration Is also called the Cori cycle Produces most of the water made in humans
Is controlled by the ADP/ATP ratio and the NADH concentration
118
The Krebs Cycle begins when pyruvic acid produced by glycolsis enters the cytosol air mitochondrion nuclear
mitochondrion
119
In aerobic organisms growing in the presence of oxygen, the NADH produced by glycolysis ultimately donates its high-energy electrons to electron transport chains in the mitochondria ATP pyruvate glucose
electron transport chains in the mitochondria
120
Cellular respiration takes place mostly in: chloroplasts ribosomes nucleus mitochondria
mitochondria
121
The main purpose of the electron transport chain is to: Use high energy electrons from other cycles to convert ADP into ATP Maintain a stable balance of high energy electrons Constantly distribute electrons throughout the cell Tell the cell when glycolysis should stop or start
Use high energy electrons from other cycles to convert ADP into ATP
122
Oxidative phosphorylation: Is anaerobic Requires AMP Requires the electron transport system Is not dependent upon development of a proton gradient
Requires the electron transport system
123
Where are the proteins of the electron transport chain located? cytosol mitochondrial outer membrane mitochondrial inner membrane mitochondrial matrix
mitochondrial inner membrane
124
The ATP synthase responsible for most of the ATP synthesis in the body is located: On the outer side of the outer mitochondria membrane On the inner side of the outer mitochondria membrane On the outer side of the inner mitochondria membrane On the inner side of the inner mitochondria membrane
On the inner side of the inner mitochondria membrane
125
In the electron transport chain, the final electron acceptor is oxygen a molecule of carbon dioxide a molecule of water ADP
oxygen
126
Anemia, hemorrhage, and chronic obstructive pulmonary disease can all cause metabolic acidosis. The best explanation is that the lack of oxygen causes a decrease in insulin that, in turn, increases anaerobic glycolysis in the brain a decrease in oxidative phosphorylation so the cells have to rely upon anaerobic glycolysis a decrease in the removal of CO2 from the blood. The resulting decrease in pH causes an increase in glycolysis in most cells an increase in glycolysis in red blood cells
a decrease in the removal of CO2 from the blood. The resulting decrease in pH causes an increase in glycolysis in most cells
127
Hydrolysis of a triglyceride produces many amino acids different types of nucleotides fatty acids and glycerol monosaccharides
fatty acids and glycerol
128
The site of amino acid catabolism is the: Stomach Small intestine Large intestine Liver
Liver
129
The first step in the catabolism of most amino acids is Removal of carboxylate groups Enzymatic hydrolysis of peptide bonds Removal of the amino group Zymogen cleavage
Removal of the amino group
130
Which of the following is true of urea? more toxic to human cells than ammonia the primary nitrogenous waste products of humans. insoluble in water the primary nitrogenous waste product of most aquatic invertebrates
the primary nitrogenous waste products of humans.
131
A glucogenic amino acid is one which is degraded to keto-sugars either acetyl CoA or acetoacetyl CoA pyruvate or citric acid cycle intermediates none of the above
pyruvate or citric acid cycle intermediates
132
Transamination is the process where carboxyl group is transferred from amino acid α-amino group is removed from the amino acid polymerization of amino acid takes place none of the above
α-amino group is removed from the amino acid
133
Transamination is the transfer of an amino acid to a carboxylic acid plus ammonia group from an amino acid to a keto acid acid to a keto acid plus ammonia group from an amino acid to a carboxylic acid
group from an amino acid to a keto acid
134
In inherited deficiency of hypoxanthine guanine phosphoribosyl transferase De novo synthesis of purine nucleotides is decreased Salvage of purines is decreased Salvage of purines is increased Synthesis of uric acid is decreased
Salvage of purines is increased
135
Which of the following is a required substrate for purine biosynthesis ? 5- methyl thymidine Ribose phosphate PRPP 5-Fluoro uracil
PRPP
136
The conversion of Inosine mono phosphate To Adenosine mono phosphate (AMP) is inhibited by Guanosine mono phosphate (GMP) To AMP requires uridine mono phosphate (UMP) To GMP requires GMP kinase To GMP requires Glutamine
To GMP requires Glutamine
137
Both strands of DNA serve as templates concurrently in replication excision repair mismatch repair none of these
replication
138
Proofreading activity to maintain the fidelity of DNA synthesis occurs after the synthesis has been completed is a function of the 3'-5' exonuclease activity of the DNA polymerases requires the presence of an enzyme separate from the DNA polymerases occurs in prokaryotes but not eukaryotes
is a function of the 3'-5' exonuclease activity of the DNA polymerases
139
Which of the following repairs nicked DNA by forming a phosphodiester bond between adjacent nucleotides? Helicase DNA gyrase Topoisomerases DNA ligase
DNA ligase ## Footnote DNA ligase repairs nicked DNA
140
The replication of chromosomes by eukaryotes occurs in a relatively short period of time because the eukaryotes have more amount of DNA for replication the eukaryotic replication machinery is 1000 times faster than the prokaryotes each chromosome contains multiple replicons eukaryotic DNA is always single stranded
each chromosome contains multiple replicons
141
During which of the following process a new copy of a DNA molecule is precisely synthesized? Trasformation Transcription Translation Replication
Replication
142
Which of the following enzyme adds complementary bases during replication? Helicase Synthesase Replicase Polymerase
Polymerase
143
Which of the following enzymes unwind short stretches of DNA helix immediately ahead of a replication fork? DNA polymerases Helicases Single-stranded binding proteins Topoisomerases
Helicases
144
Which DNA polymerase removes RNA primers in DNA synthesis? Polymerase I Polymerase II Polymerase III none of these
Polymerase I
145
Enzyme, responsible for proofreading base pairing is DNA polymerase Telomerase Primase DNA lig
DNA polymerase ## Footnote PP proofreading polymerase
146
DNA helicase is used to unwind the double helix interact the double helix closely break a phosphodiester bond in DNA strand none of the above
unwind the double helix
147
The synthesis of DNA by DNA polymerase occurs in the 3' to 5' direction 5' to 5' direction 5' to 3' direction 3' to 3' direction
5' to 3' direction
148
The 5' and 3' numbers are related to the length of the DNA strand carbon number in sugar the number of phosphates the base pair rule
carbon number in sugar
149
What is the main damaging effect of UV radiation on DNA? Depurination Formation of thymine dimers Single strand break Dehydration
Formation of thymine dimers
150
Which of the following enzyme is used for synthesis of RNA under the direction of DNA? RNA polymerase DNA ligase DNA polymerase RNA ligase
RNA polymerase
151
Which of the following is a product of transcription? mRNA tRNA rRNA all of these
all of these
152
Recognition/binding site of RNA polymerase is called receptor promoter facilitator terminator
promoter
153
An mRNA transcript of a gene contains a start codon a stop codon a terminator all of these
all of these
154
Where in the cell is the DNA transcribed into mRNA? Cytoplasm Nucleus Golgi Cell cytoskeleton
Nucleus
155
Since the two strands of the DNA molecule are complementary, for any given gene: The RNA polymerase can bind to either strand. Only one strand actually carries the genetic code for a particular gene. Each gene possesses an exact replica so that no mutation occurs. A gene transcribed in the 5’ to 3’ direction on one strand can be transcribed in the 3’ to 5’ direction on the other strand.
Only one strand actually carries the genetic code for a particular gene.
156
The site of protein synthesis is Ribosome Nucleus Endoplasmic reticulum Chromosome
Ribosome
157
The structure in a bacterium that indicates an active site for protein synthesis is a chromosome. a cell membrane, a flagellum. a polysome.
a polysome
158
Which of the following is not necessary for protein synthesis to occur, once transcription is completed? tRNA Ribosomes mRNA DNA
DNA
159
During the process of translation: the peptide is ‘passed’ from the tRNA in the P-site to the tRNA in the A-site. incoming tRNAs must first bind to the E-site. initiation begins with the binding of the ribosomal SSU to the poly-A tail of the mRNA. the mRNA is translated by one ribosome at a time
the peptide is ‘passed’ from the tRNA in the P-site to the tRNA in the A-site.
160
The nucleolus of the nucleus is the site where: RNA processing occurs rRNA is transcribed and ribosomal subunits are assembled tRNA are charged with amino acids mRNA is translated into protein
rRNA is transcribed and ribosomal subunits are assembled
161
The ribosomes are composed of proteins RNA both (a) and (b) lipids
both (a) and (b)
162
Which is required for protein synthesis? tRNA mRNA rRNA All of these
All of these
163
In the genetic code there are: more tRNAs than codons. more codons than amino acids. more nucleotides than codons. the same number of codons and amino acids
more codons than amino acids.
164
the anticodon of tRNA binds to rRNA binds to an amino acid binds to the Shine Dalgarno sequence binds to an mRNA codon
binds to an mRNA codon
165
Initiation of eukaryotic translation begins when the: large and small subunits link together, then bind tothe mRNA. ribosomal small subunit holding an initiator tRNA binds to the 5’ end of mRNA. ribosome binds to of the start codon and an initiator tRNA enters the ribosome. initiator tRNA binds to the start codon, followed by binding of the ribosome large subunit.
ribosomal small subunit holding an initiator tRNA binds to the 5’ end of mRNA
166
On the ribosome, mRNA binds between the subunits to the large subunit to the small subunit none of these
to the small subunit
167
Ribosomes select the correct tRNAs based on the aminoacyl group solely on the basis of their anticodons depending on their abundance in the cytosol with the least abundant anticodons
solely on the basis of their anticodons
168
Which of the following amino acid starts all proteins synthesis? Glycine Proline Thymine Methionine
Methionine