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BCH 203 STUDY QUESTIONS & ANSWERS

1. The following is true of enzymes except…


A. They are insensitive to pH.
B. Are proteins that alter the rate of chemical reaction in a living system.
C. They mediate the transformation form of energy into another.
D. The most striking characteristics of enzymes are their catalytic power and
specificity.
2. Catalysis takes place at a particular site on the enzyme called…

3. Normally, all enzymes are … however, proteins do not have an absolute monopoly on
catalysis.

4. Enzymes regulate biological processes within all living organism. T/F.

5. Enzymes catalyzes all of cell metabolism. T/F

6. The conversion and transformation of chemical energy and the construction of cellular
macromolecules from smaller precursors is possible by the activities of …

7. Many inherited human diseases such as Albinism & PKU results from the overproduction of a
particular type of enzyme. T/F.

8. An enzyme molecule is composed of one or more amino acid chains called…

9. If the enzyme is subjected to change in temperature or pH, the protein may loose its
enzymatic ability and…

10. The following is true about co-factors except.


A. The co-factor is referred to as a prosthetic group if tightly connected to the enzyme.
B. Co-factor may not be a co-enzyme.
C. May be either a co-enzyme which is an organic molecule or an inorganic metal ion.
D. A co-factor may be either tightly or loosely bound to the enzyme.

11. An enzyme will interact with only one type of substance or group of substances called the
…, to catalyse a certain kind of reaction.

12. List the 6 principled categories of enzymes.

13. ...is involved in electron transfer.


A. Transferase
B. Oxido-reductases
C. Hydrolases
D. Lyases
14. Hydrolases cleaves the substrate by uptake of a water molecule (hydrolysis). T/F

15. Isomerases form double bonds by adding or removing a chemical group. T/F

16. ...or ...couple the formation of various chemical bonds to the breakdown of a pyrophosphate
bond in ATP or a similar nucleotide.

17. Write out the catalytic properties of enzymes.

18. The substrate-specificity of enzymes is based on amino acid sequence in the the catalytic
site as well as the optical isomeric form of the substrate. T/F.

19. List the properties of enzymes

20. All enzymes are proteins except


A. Ribozyme
B. Aldolase
C. Epimerase
D. Hexokinase.

21. The colloidal nature of enzymes doesn't enable it to be isolated by dialysis. T/F

22. Enzyme efficiency (Turnover number) is the number of substrate molecules changed per
unit of time per enzyme. T/F.

23. Turnover number for the following enzymes is correct except:


A. Carbonic anhydrase is 36million
B. Catalase is 6million
C. Sucrase is 10,000
D. Very low in lysosyme

24. Enzymes are sensitive to changes in the following except:


A. pH
B. Temperature
C. Inhibitors
D. Volume

25. Enzymes work best at a narrow range of conditions called…

26. The optimum temperature of enzymes is 20°-35°C. T/F

27. High molecular weight enzymes are comparatively more heat stable. T/F.
28. The following is true concerning pH of enzymes except.
A. Optimum pH of most endoenzymes is pH 5.0
B. Salivary amylase acts best at pH 6.8
C. Pepsin act at pH 1-2
D. Alkaline phosphatase at pH 10-11.
E. Sometimes a change in pH will cause the reverse reaction.
F. Acid phosphatase at 4-6

29. Enzymes are sensitive to inhibtors. T/F

30. … are any molecule like cellular metabolites, drugs or toxins which reduce or stop enzyme
activity.

31. The following are irreversible inhibitors except.


A. Uncompetitive inhibitors.
B. Noncompetitive inhibitors
C. Mixed inhibitors
D. Allosteric or feedback inhibitors.

32. Concerning reversible inhibitors:


A. A competitive inhibitor competes with a substrate to irreversibly bind to its active/catalytic
site. T/F.
B. The action of competitive inhibitor is overcomed by increasing substrate concentration.
T/F.
C. Uncompetitive inhibitor binds reversibly to the enzyme-substrate complex not to the free
enzyme. T/F.
D. Malonate is an uncompetitive inhibitor which competes with succinate and inhibits the
activity of succinate dehydrogenase. T/F.

33. Concerning irreversible inhibition:


A. They covalently bind to amino acid residues at catalytic sites and permanently
inactivates the enzymes. T/F
B. Penicillin covalently binds to serine residue in the active sites of glycopeptide
transpeptidase enzyme which forms cross-linking in bacteria cell wall. T/F.
C. Noncompetitive inhibitor doesn't bind to both the free enzyme and the enzyme-substrate
complex. T/F
D. Noncompetitive inhibition is when the end-product of a metabolic pathway inhibits the
activity of the first enzyme of that pathway. T/F.

34. What are the factors affecting enzymes activity?

35. As the concentration of enzyme increases, the velocity of the reaction proportionally…
36. Increase in substrate concentration gradually increases the velocity of the enzyme reaction
within the limited range of substrate level. T/F

37. A Bell-shaped curve is obtained with effect of temperature on enzymes. T/F

38. The optimum temperature for most of the enzyme will be


A. 35-60°C
B. 20-40°C
C. 40-45°C
D. 60-70°C

39. Th accumulation of reaction products generally increases the enzyme velocity. T/F

40. Metalloenzymes are those enzymes that require certain metal ions for their activity. T/F

41. Concerning enzyme kinetics. T/F


A. The measure of enzyme activity in living systems.
B. Addresses the biological role of enzymatic catalyst and how the accomplish their
remarkable feats.
C. Seeks to determine the maximum reaction velocity that the enzyme can attend and its
binding affinity to substrate and inhibitors.
D. Drugs are special activators specifically targeted at a particular enzyme inorder to
overcome infection or to annihilate illness.

42. ...is defined as the substrate concentration (in mol/litre) to produce ½ maximum velocity of
an enzyme catalyzed reaction.
A. Vmax
B. Km
C. K
D. 1/2Vmax

43. Which is not true concerning Km


A. Km value is a constant and a characteristic feature of a given enzyme.
B. It is a representative of measuring the strength of ES complex.
C. A high Km indicates a strong affinity between enzyme and substrate.
D. A high Km indicates weak affinity between enzyme and substrate.

44. What is allosteric regulation of enzymes?

45. Allosteric enzymes have an ...site where substrate bind and ...site where the modifier binds.

46. An … site does not bind/accommodate substrate but instead it binds another molecule that
affects the enzyme regulation.
47. The activation state of the enzyme is the "R" group or the relaxed state, when the enzyme is
off and its activity turned down. T/F.

48. In the "T" or Tense state, the enzyme is off and its activity is turned down. T/F.

49. ...are the non-protein components of enzymes and maybe metal ions or organic molecules
referred to as coenzymes.
A. Prosthetic group
B. Cofactors
C. Allosteric enzymes
D. Apoenzymes

50. Cofactors tend to be stable to heat because they are structurally less complex than proteins.
T/F

51. Concerning coenzymes. T/F


A. Many coenzymes are carbohydrates
B. Are actively involved in the catalytic reaction of the enzyme
C. Doesn't serve as intermediate carriers of functional groups in convention of substrate
product.
D. Firmly associated with its enzyme by hydrolytic bonds and is difficult to separate the two.

52. Some tightly bound coenzymes are referred to as …

53. The catalytically active complex of protein and prosthetic group is called
A. Cofactors
B. Apoenzyme
C. Holoenzyme
D. Vitamins

54. The protein without a prosthetic group is called…

55. Coenzymes serves as recyclable shuttle or group transfer agents that transport many
substrate from their point of generation to their point of utilization. T/F

56. Other chemical moiety transported by coenzymes except


A. Methyl groups (Retinoic acid)
B. Acyl groups (Coenzyme A)
C. Oligosaccharides
D. Methyl groups (Folates)

57. List other examples of coenzymes


ANSWERS
1. A
2. Active site
3. Proteins
4. T
5. T
6. Enzymes
7. F
8. Polypeptides or polypeptide chain
9. Denature
10. B
11. Substrate
12. Oxido-reductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase (OTHLIL).
13. B
14. T
15. F
16. Ligases or synthetases
17. .
18. T
19. .
20. A
21. F
22. T
23. B
24. D
25. Optimum conditions
26. T
27. F
28. A
29. T
30. Inhibitors
31. A
32. F, T, T, F
33. T, T, F, F
34. .
35. Increases
36. T
37. T
38. C
39. F
40. T
41. T, T, T, F
42. B
43. C
44. .
45. Active site, Allosteric site
46. Allosteric site
47. F
48. T
49. B
50. T
51. F, T, F, F
52. Prosthetic group
53. C
54. Apoenzyme
55. T
56. A
57. .

58. Out of the 300 amino acids present in plants, animals, and microbial system, only about
20 are coded by DNA to appear in proteins. T/F.

59. … are the basic structural units of proteins consisting of an amino group (-NH2), a
carboxyl group (-COOH), a hydrogen (H) atom and a (variable) distinctive( R) group. All
of the substituents in amino acid are attached to a central ...

60. Write out the general structure of alpha-amino acids identifying it's alpha carbon atom.

61. A tetrahedral carbon atom with 4 distinct constituents is said to be …

62. … describes the handedness of a molecule to rotate the plane of polarized light either to
the right (dextrorotary) or to the left (levorotatory).
A. Polarity
B. Chirality
C. Enantiomers
D. Zwitterion

63. The class of stereoisomers that are non-superimposable mirror images of each other are
called…
A. Dextrorotary
B. Levorotatory
C. Enantiomers
D. Zwitterions

64. Enantiomeric molecules exhibit a special property called … -the ability to rotate plane of
polarization of plane-polarized light.
65. Only D-amino acids are constituents of proteins. T/F

66. Glycine and B-alanine are optically active. T/F

67. Concerning Zwitterions T/F


A. The carboxyl group is deprotonated to a carboxylate ion, and the amino group is
protonated to ammonium ions.
B. Amino acids in solution at neutral pH exist predominantly as dipolar ions.
C. Has a net charge of 7
D. Are substances containing equal numbers of positive and negative charge.

68. Define the isoelectric point.

69. An amino acid with no ionizable R-group would be electrically neutral at physiological pH
(around 7.4) is termed a …

70. Which of this is not true of amino acids. T/F


A. Amino acids are readily soluble in aqueous media and are only slightly soluble or
insoluble in organic solvents.
B. High boiling point (200°C)
C. Thought to exist in natural solution as doubly-charged ions known as zwitterions.
D. Are amphoteric (have both acidic and basic properties).

71. … is the negative logarithm of Ka.

72. Calculate the isoelectric pH (pI) of alanine given that the first pKa (R-COOH) is 2.35 and the
second pKa (R-NH3) is 9.69.
A. 3.00
B. 2.8
C. 6.02
D. 1.02

73. The pK value of imidazolium group of … is 6.1, and therefore effective as a buffer at the
physiological pH of 7.4.

74. Which amino acid has imidazole ring?

75. Give the names of the two Amide amino acids.

76. Guanidino group is seen in …

77. Draw one amino acid each with Imino group, acidic group, indole group and aliphatic R-
group.
78. Nonpolar amino acids are hydrophobic. T/F

79. … amino acids have side chains that contain an amino group that can ionize as a weak
base.

80. Essential amino acids are…

81. … and… are semi-essential amino acids.

82. … amino acids have carbon skeleton that can be converted to glucose and glycogen.

83. ...and … two exclusively ketogenic amino acids.

Anwers

58. T
59. Amino acids, alpha carbon atom.
60. …
61. Chiral
62. B
63. C
64. Optical activity
65. F
66. F
67. T, T, F, T
68.
69. Zwitterions
70. F, T, F, F
71. pKa
72. C
73. Histidine
74. Histidine
75. Asparagine, Glutamine
76. Arginine
77.
78. T
79. Acidic amino acids
80.
81. Arginine, Histidine
82. Glucogenic
83. Leucine, Lysine.

84. Which of this is not true about water.


A. Water constitute less than 50% of animal tissues.
B. It is the main solvent of living organisms.
C. Water has the ability to polarize and the tendency to ionize.
D. It is a covalent compound in which an atom of Oxygen is linked to two atoms of
Hydrogen.

85. A … is a molecule having electrical charge distributed asymmetrical about its structure.
A. Enantiomer
B. Dipole
C. Polar
D. Diasteromer

86. The dipole structure of water makes it…


A. Non polar
B. Polar

87. Solubility of water. T/F


A. Biological substances that dissolve in water are nonpolar.
B. Amino acids, carbohydrates, and nuclei acids have a number of polar groups that allow
them to dissolve in water.
C. Lipids are nonpolar hence cannot dissolve in water.
D. The dipole property of water is responsible for its high dielectric constant
( 78.5 at 25°C)

88. Hydrogen bonding property of water accounts for its lower melting point, boiling point and
heat of vaporization. T/F

89. The ability of water to form hydrogen bonding with other biomolecules partly accounts for its
ability to dissolve many organic substances. T/F

90. What is pH?

Answers
84. A
85. B
86. B
87. F, T, T, T
88. F
89. T

91. An acid is a substance that can donate proton and a base is a substance that can accept
protons. T/F.

92. A base reacts with H2O to form the conjugate base of the acid and the conjugate acid of the
base. T/F.
93. The strength of an acid is specified by its dissociation constant. T/F.

94. Weak acids have K>1 and are almost completely ionized in aqueous solution. T/F.

95. The following are strong acids except


A. H2SO4
B. CH3COOH
C. HCL
D. HNO3

96. The pH of a solution can be accurately and easily determined through electrochemical
measurements with a device known as …

97. The pH of a solution is determined by the relative concentration of acids and bases. T/F.

98. Write out the Henderson-Hasselbach equation.

99. The … equation shows that the pK of an acid is numerically equal to the pH of the solution
when the molar concentrations of the acid & conjugate base are equal.

100. The pH range over which a solution can function effectively as a buffer is known as …

101. Write short note on Buffers.

102. Substances that bear more than one acid-base groups such as H3PO4, H2CO3, as well as
most biomolecules are known as …

Answers

91. T
92. F
93. T
94. F
95. B
96. pH meter
97. T
99. Henderson- Hasselbach equation
100. Buffering capacity
102. Polyprotic acids.

103. … are polymers of amino acid linked through a polypeptide bond.


104. ...bond is made up of the carboxyl group of the first amino acid and the amino group of the
next amino acid.

105. Draw a peptide bond.

106. Proteins can be classified based on the following except


A. Composition & solubility of proteins.
B. Functions
C. Shape & size
D. Structure
E. Nutritive values

107. Complex proteins yield only amino acid on hydrolysis. T/F

108. Fibrous proteins are insoluble in all common solvents. T/F

109. The following are globular proteins except


A. Keratin
B. Prolamines
C. Albumin
D. Histones

110. The protein component of conjugated proteins is called… while the non protein component
is called the …

111. … do not exist in nature but are gotten from natural proteins by the action of various
physical & chemical agents.

112. Peptide bonds of Primary-derived proteins are not broken while the progressive or
enzymatic hydrolysis of peptide bonds yield Secondary-derived proteins. T/F

113. Peptides can be precipitated from solution by phosphotungistic acid. T/F

114. All enzymes except… are protein in nature.

115. The following are signal transduction proteins except


A. Immunoglobulin
B. G-protein
C. Adenylate cyclase
D. Guanylate cyclase

116. The axial ratio of length: width is less than 10 for globular proteins. T/F

117. Complete, partially complete and incomplete proteins are classified on the basis of their…
118. Write on the general properties of proteins

119. ...is the lose of the native conformation of protein, due to unfolding and disorganisation of
secondary, tertiary and quartenary structure of protein.

120. The precipitation of proteins from their solution by applying heat is known as heat
coagulation. T/F

121. The pH at which the net charge of the protein is zero is called…

122. Biuret reaction indicates the presence of two or more peptide bonds. T/F

123. Millions reaction gives a red coloured complex which indicates the presence of ...group.
A. Indole ring.
B. Phenol
C. Thiol
D. Benzene ring.

124. Nitroprusside reaction gives a red coloured complex which indicates the presence of thiol
group specific for …

125. Write on the structural organization of proteins.

126. ...structure refers to the linear sequence of amino acids linked together through peptide
bond.
A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure.

127. Alpha-helix and Beta-pleated sheaths are types of ...structure of protein.

128. How many subunits are present in the following proteins.


A. Creatinine phosphokinase…
B. Aldolase…
C. Hemoglobin…
D. Lactate dehydrogenase…

129. Proteins with two or more polypeptide chains (subunits) have a …

130. Van der Waals forces are very strong forces that develop between non-polar side chains of
neutral amino acids. T/F
131. Replacement of Glutamine for Valine at position six of beta-globin chains of hemoglobin
form sickled-shaped hemoglobin. T/F.

Answers

103. Proteins
104. Peptide bonds
105.
106. D
107. F
108. T
109. A
110. Apoprotein, prosthetic group.
111. Derived proteins
112. T
113. T
114. Ribozymes
115. A
116. T
117. Nutritive values
118.
119. Denaturation
120. T
121. Isoelectric pH/ Isoelectric point pI
122. T
123. B
124. Cysteine
125.
126. A
127. Secondary
128. A. 2, B. 3, C. 4, D. 5.
129. Quaternary structure
130. F
131. T

132. Peptides are involved as neurotransmitters, neuromodulators and hormones in receptor-


mediated signal transduction. T/F

133. The following are importance of peptides except


A. As potential intrinsic drugs for the treatment of pathologic process.
B. Synthetic peptides serve as antigens to raise antibodies.
C. As enzyme substrates
D. As enzyme inhibitors.
134. ...bond is also called the peptide bond. It has a partial double bond-like characteristic that
prevents free rotation.

135. T/F
A. Oligopeptides composed less than 10 amino acids.
B. Polypeptides has approx. 15-50 amino acids
C. Proteins have greater than 50 amino acids.

136. The number and sequence of amino acid that are connected to a peptide or a protein are
called the …
A. Secondary structure
B. Tertiary structure
C. Primary structure
D. Quaternary structure

137. The primary structure is the raw sequence of amino acid. T/F

138. A disulfide bond between two thiol groups of cysteine is formed upon oxidation to give a
cysteine residue. T/F

139. Describe the steps in protein isolation.

140. Extraction is the process of getting proteins out of the cell and subcellular organelles. It
involves two steps;...and …

141. ...is the rupture of the cell membrane resulting in the release of cell contents, and the
subsequent death of the cell. It is usually done in a buffered solution in order to protect the
integrity of the protein.

142. The following are methods of homogenization. T/F


A. Physical method: osmotic shock, freeze/thaw
B. Chemical method: detergent, organic solvents, alkali
C. Enzymatic method: lysozme
D. Mechanical method: blending, French press, mortar & pestle, glass homogenizers.
E. Ultrasonic vibration: sonicator.

143. Conditions for homogenization. T/F


A. High temperature (>4°C)
B. Buffer with pH ~ 7.0-7.4
C. Chelating agent (EDTA)
D. Reducing agent (mercaptoethanol).

144. ...is the 2nd step of extraction to get rid of debris.


A. Purification
B. Homogenization
C. Centrifugation
D. Gel electrophoresis

145. In differential centrifugation, separation is based on ...and …

146. The two media used for density gradient centrifugation are … and …

147. The two phases of chromatography are ...and…

148. Separation is based on ...with Gel-filtration chromatography.


A. Density
B. Charge
C. Size
D. Shape.

149. With affinity chromatography, the protein binds to … in the mobile phase and is recovered
from the column.
A. Electrode
B. Ligand
C. Receptor
D. Sucrose

150. In Ion-exchange chromatography, a negatively charged resin is a ...exchanger while a


positively charged resin is ...exchanger.

151. ...uses very high resolution columns that can be run under high pressures. And is usually
very fast.
A. High pressure liquid chromatography
B. Gel-filtration chromatography
C. High Performance liquid chromatography
D. Ion-exchange chromatography

152. Gel electrophoresis is based on electric charge. T/F.

ANSWERS

132. T
133. F, F, F, F
134. Omega bond
135. F, T, T
136. C
137. T
138. T
139
140. Homogenization, Centrifugation
141. Homogenization
142. T, T, T, T, T
143. F, T, T, T
144. C
145. Size and density
146. Sucrose medium, Optiprep medium
147. Mobile phase, stationary phase
148. C
149. B
150. Cation exchanger, Action exchanger.
151. C
152. T

1. Write out the central dogma

2. The mechanism whereby inherited information is used to create actual objects, namely
enzymes and structural proteins is …

3. …is an exception to the central dogma and they make DNA from RNA by using the
enzyme…

4. …are DNA sequences that encode proteins.

5. …refers to the process whereby the information contained in genes begins to have
effects in the cell. A. Gene expression. B. Gene regression. C. Gene depression

6. …encodes and transmits the genetic information passed down from parents to offspring.
A. RNA B. DNA C. ATP

7. A nucleic acid word ( three nucleotide letters ) is referred to as a …

8. The alphabet of the genetic code contains only four letters namely…

9. Nucleic acid is a linear polymer of nucleotides. T/F

10. The principle information in the cell is the …and all genetic codes at carried out on it.

11. …are the unit structure of nucleic acids. A. Nucleotide. B. Nucleosides.

12. Nitrogenous base + Pentose sugar + Phosphate = A. Nucleotide. B. Nucleoside.


13. The two types of nitrogenous bases are … and …

14. The following are purine except A. Thymine. B. Adenine. C. Guanine.

15. Cytosine, Uracil, and Guanine are all examples of pyrimidine. T/F.

16. The two types of nucleic acids are …

17. DNA has OH at 2’ position. T/F

18. Uracil is found only in RNA. T/F

19. Nucleotides polymerize together by phosphodiester bonds through condensation


reaction. T/F

20. The phosphodiester bond is formed between. A. Hydroxyl group of the sugar of one
nucleotide. B. Phosphate group of other nucleotide. C. A and B. D. B only

21. Polynucleotide chains are always synthesized in the 5’ to 3’ direction. T/F

22. A=T T/F

23. G=C T/F

24. Which form of DNA is left-handed. Is GC rich DNA regions A. B-form. B. A-form. C. Z-
form

25. The A-form DNA is more common in RNA. T/F

26. GC regions denature first. T/F

27. Hyperchromicity is used to measure the DNA denaturation and annealing. T/F

28. … carries genetic material as codon. A. tRNA. B. mRNA. C. rRNA.

29. tRNA is specific to each amino acid. T/F

30. … catalyse the assembly of amino acid into proteins. A. tRNA. B. mRNA. C. rRNA.

31. The tertiary structure of RNA is … A. Motifs and 3D folding. B. Hairpin loops. C.
Sequence of nucleotides.
32. Replication of DNA is … A. Discrete B. Semi-conservative. C. Constant.

33. … is the enzyme that brings the substrates to the DNA strand template; it adds
nucleotides to the 3’ end of the primer.

34. Nucleotides are always added to the growing strand at the 3’end. T/F

35. The hydroxyl group reacts with the phosphate group on the 5’C of the deoxyribose so
the chain grows. T/F

36. … unwinds and opens DNA strands for replication. A. DNA polymerase I. B. Helicases.
C. Ligase.

37. Synthesis of new DNA strands occur in both directions. T/F

38. List the 3 steps of DNA replication

39. The helper strand needed to start a new strand of DNA is called … A. Telomerase. B.
Ligase. C. Primer.

40. Primer is a short, single strand of RNA and is complimentary to the DNA template
strand. T/F

41. … catalyzes the elongation of new DNA strands in prokaryotes. A. DNA polymerase I. B.
DNA polymerase II. C. DNA polymerase III.

42. Strand elongation is from A. 5’ to 3’ B. 3’ to 5’ C. 4’ to 3’

43. The second daughter strand is usually antiparallel to the leading strand. T/F

44. When an Okazaki fragment forms, … removes the RNA primer and replaces it with DNA
adjacent to the fragment. A. DNA polymerase I. B. DNA polymerase II. C. DNA polymerase III.

45. DNA ligase catalyzes the final bond T/F

46. … is a reverse transcriptase that prevents shortening of lagging strands during DNA
replication. A. Telomerase. B. Ligase. C. Primer.

Answers
1. DNA > RNA >Protein
2. Central dogma
3. Retroviruses
4. Gene
5. Gene expression
6. B
7. Codon
8. ACTG
9. T
10. Nuclei acids
11. A
12. A
13. Purine and Pyrimidine
14. A
15. F
16. DNA & RNA
17. F
18. T
19. T
20. C
21. T
22. T
23. F
24. C
25. T
26. F
27. T
28. B
29. T
30. C
31. A
32. B
33. DNA polymerase
34. T
35. T
36. B
37. T
38. Step 1. Unwinding and exposing strands.
Step 2. Priming the strand.
Step 3. Strand elongation.
39. C
40. T
41. C
42. A
43. T
44. A
45. T
46. A
47. …the first person to see cells, he was looking at cork and noted that he saw “a great
many boxes” (1665). A. Mattias Schleiden. B. Robert Hooke C. Anton van Leeuwenhoek

48. Rudolf Virchow predicted that cells come from preexisting cells. T/F

49. The zoologist who observed tissues of animals have cells (1839) is A. Theodore
Schwann B. Mattias Schleiden C. Rudolf Virchow

50. List the components of the cell theory

51. All cells have these parts except … A. Cell wall B. Ribosomes C. Cytoplasm D. DNA E.
Cytoskeleton F. Cell membrane

52. Bacteria cells have a cell membrane T/F

53. The cell theory was developed by a single scientist T/F

54. Cells taken from fungi do not have DNA T/F

55. … do not have a nucleus, their DNA is circular and floats in the cytoplasm. A.
Eukaryotes B. Animals C. Prokaryotes

56. Eukaryotic cells is found in the following except A. Protist B. Fungi C. Bacteria D. Plants

57. List the 4 main parts of eukaryotic cell

58. Nucleus contains cell’s DNA in the two forms of … and …

59. A vesicle is used with the Golgi to transport substances outside cell, like a messenger
delivering a package. T/F

60. Lysosome is described as A. Powerhouse B. Suicide sac C. Center of cell

61. Endoplasmic reticulum transport “intracellular highway” T/F

62. Mitochondria and chloroplasts lack their own DNA. T/F


63. … states that eukaryotic cells evolved when prokaryotic cells engulfed or absorbed other
cells. A. Cell theory B. Central dogma C. Endosymbiosis theory.

Answers
47. B
48. T
49. A
50. a. Every living organism is made of one or more cells
b. The cell is the basis unit of structure and function.
c. It is the smallest unit that can perform life functions.
d. All cells arise from preexisting cells.
51. A
52. T
53. F
54. F
55. C
56. C
57. Cell membrane, cytoplasm, nucleus, organelles.
58. Chromatin & chromosome
59. T
60. B
61. T
62. F
63. C

64. … is defined as the external pressure required to be applied so that there is no net
movement of solvent across the membrane.

65. Osmotic pressure is a colligative property. T/F

66. Biological membranes are permeable to large and polar molecules and impermeable to
non-polar or hydrophobic molecules. T/F

67. … depends on solubility, charge, as well as solute size. A. Osmolality B. Permeability C.


Osmolarity

68. The factors affecting osmosis are: … and …

69. … is the measure of the effective osmotic pressure gradient; the water potential of two
solutions separated by a semipermeable cell membrane. A. Solvent B. Osmolarity C. Tonicity
70. Tonicity is influenced only by solutes that cannot cross the membrane, as only these
exert an effective osmotic pressure. T/F

71. A cell is called … if it has a greater concentration of solutes than the cytosol inside the
cell. A. Hypotonic B. Hypertonic C. Osmolar

72. The solution on either side of a cell membrane are … if the concentration of solutes
outside the cell is equal to the concentration of solutes inside the cell. . A. Hypotonic B.
Hypertonic C. Osmolar D. None of the above

73. Normal saline is almost isotonic to blood plasma. T/F

74. Donnan equilibrium relationship is derived from …

75. Donnan dialysis is particularly effective for recovery or removal of multivalent ions. T/F

Answers
64. Osmotic pressure
65. T
66. F
67. B
68. Osmotic pressure and osmotic gradient
69. C
70. T
71. B
72. D
73. T
74. Thermodynamics
75. T

76. Fat is the stored form of energy in many organisms. T/F

77. … are biological molecules which are insoluble in water and soluble in nonpolar organic
solvents A. Glucose B. Lipids C. Thymine

78. Lipids form about 3.5% of cell content T/ F

79. … is a trihydroxy sugar with three carbon atoms and three hydroxyl groups. A. Glycerol
B. Fat C. Phospholipid
80. … is seen in biological systems as an intermediate in carbohydrate and lipid metabolism.
A. Glycerol B. Fat C. Phospholipid

81. Triglycerides are also called … they are fatty acid triesters of glycerol.

82. The covalent bonds between the triglyceride molecules are called Ester bonds and are
formed during …reaction

83. … are the storage form of lipids in the adipose tissue A. Cholesterol B. Triacylglycerols
C. Phospoholipids

84. … are the building blocks of lipid and they contain carboxyl groups bound to a carbon
chain with attached hydrogen. A. Triacylglycerol B. Cholesterol C. Fatty acids.

85. All natural lipids yield … on their hydrolysis

86. The alkyl chain of saturated fatty acid has double bonds. T/F

87. Palmitic acid has … carbons A. 20 B 18. C. 16

88. Stearic acid has … carbons A. 20 B 18. C. 16

89. Linoleic acid and Linolenic acid are … fatty acids. A. Nonessential B. Essential

90. The presence of single bonds in unsaturated fatty acids make them relatively more
reactive than saturated fatty acids. T/F

91. Diets rich in … such as vitamin C, E, A and Selenium, reduce lipid peroxidation.

92. The following are the three major groups of lipids except … A. Simple lipid B. Complex
lipids C. Saturated lipids D. Derived lipids

93. These are complex lipids except A. Waxes B. Phospholipids C. Glycolipids D.


Sulpholipids

94. … are most abundant in white matter of brain and myelin sheath. A. Sulpholipids. B.
Proteolipids C. Phospholipids

95. Derived lipids except A. Glyceryl esters B. Cholesterol C. Eicosanoids Fatty acids.

96. Sphingolipids play a role in cytokinesis during interphase. T/F

97. … are natural detergents synthesized in the liver and secreted into bile. A. Fatty acids B.
Bile salts C. Phospholipids
98. Trans fat is healthy to cardiovascular health. T/F

99. Biological membranes contain … lipids, … proteins and … carbohydrates.

100. The lipid bilayer of cell membrane act as semipermeable membrane. T/F

Answers

76. T
77. B
78. T
79. A
80. A
81. Neutral fats
82. Condensation
83. B
84. C
85. Fatty acids
86. F
87. C
88. B
89. B
90. F
91. Antioxidant
92. C
93. A
94. A
95. A
96. T
97. B
98. F
99. 40%, 60%, 1-10%
100. T

101. The rate of a chemical reaction is directly proportional to the product of the activities or
concentrations of the reactants. A. Law of thermodynamics B. Law of gravity. C. Law of mass
action.

102. Gibbs change in free energy (∆G) is that portion of the total energy change in a system
that is available to do work. T/F
103. … is a function of enthalpy and entropy A. G B. ∆G° C ∆G°’

104. Entropy is a measure of the energy (heat content) while Enthalpy is a measure of
randomness of the system. T/F

105. If ∆G > 0 the reaction is A. Exergonic B. Equilibrium C. Endergonic

106. The change in free energy for going from standard conditions to equilibrium can be
written as: A. ∆G° = -RTInkeq B. G = H-TS C. ∆G = ∆G° + RT

107. In practice, endergonic process can exist independently. T/F

108. Exergonic reaction is thermodynamically feasible. T/F

109. For a coupled reaction to be thermodynamically feasible, the exothermic reactions must
be sufficiently larger than endothermic since heat will be lost from the exothermic reactions. T/F

110. The standard free energy change for ATP is A. Large and negative. B. Small and
positive. C. Large and negative.

111. … play a central role in energy capture and transfer for sustenance of living system.
A. Low-energy compounds. B. High-energy compounds.

112. … plays a major role in the transference of free energy from the exergonic to the
endergonic processes. A. AMP B. ATP C. ADP.

Answers

101. C
102. T
103. A
104. F
105. C
106. A
107. F
108. T
109. T
110. C
111. B
112. B

113. Glucose has … chiral centers in Fischer projection. A 3. B. 4. C. 6


114. All naturally occurring sugars exist as L-sugars. T/F

115. … are polyhydroxy carbonyl compounds and their derivatives. A. Amino acids. B.
Nucleotides. C. Carbohydrates.

116. Glyceraldehde is … A. Aldohexose. B. Ketotriose. C. Aldotriose

117. … and dihydroxyacetone are the simplest carbohydrates and are found as intermediates
of metabolic pathways A. Glyceraldehyde B. Ribose. Fructose.

118. … and … are almost exclusively dependent on carbohydrates as the energy source.

119. … are carbohydrate polymers and are structural components of many organisms.
A. Cellulose. B. Glycan. C. Starch

120. Cn(H20)n is the general molecular formula of …

121. Glucose + Fructose = A. Maltose. B. Galactose. C. Sucrose.

122. The enzyme that catalyze the conversion of an aldose sugar to its ketose isomer is
called …

123. D-Fructose is levorotatory while D-glucose is dextrorotary. T/F

124. … is a phenomenon in which compounds have same chemical formula but different in
the spatial arrangement of their substituents.

125. Enantiomers are stereoisomers that are non-superimposable mirror images of each
other. T/F

126. … are stereoisomers that are not mirror images of each other.

127. Mannose is an epimer of glucose at carbon A. 4. B. 5. C. 2

128. More than 99% of glucose exist in … form. A. Furanose. B. Pyranose. C. Boat

129. The process of converting one ring form to another is called …

130. The following are amino acid derivatives of simple hexoses except. A. Uronic acid.
B. Muramic acid C. Glucosamine

131. Maltose has alpha(1-4) bond while cellobiose has beta(1-4) bond. T/F
132. Sucrose is a reducing sugar. T/F

133. Examples of homopolysaccharides except A. Chondroitin sulfate. B. Starch. C.


Glycogen

134. Amylose is … while amylopectin is both linear and branched.

135. Humans have enzymes that can hydrolyze the beta(1-4) glycosidic bond in cellulose. T/F

Answers

113. B
114. F
115. C
116. C
117. A
118. Brain cells and RBC
119. B
120. Carbohydrates
121. C
122. Isomerase
123. T
124. Stereoisomerism
125. T
126. Diastereomers
127. C
128. B
129. Mutarotation
130. A
131. A
132. F
133. A
134. Unbranched
135. F

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