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Amino Acids
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on
“Biosynthesis of Amino Acids”.
Answer: d
Explanation: α-ketoglutarate is the precursor for arginine.
Answer: a
Explanation: α-ketoglutarate is the precursor for glutamate and proline. 3-phosphoglycerate is
the precursor for serine.
Answer: a
Explanation: Proline is the cyclized derivative of glutamate.
4. Precursor of glycine is
a) Proline
b) Glutamine
c) Serine
d) Glutamate
View Answer
Answer: c
Explanation: Precursor of glycine and cysteine is serine.
Answer: d
Explanation: Methionine, threonine, lysine, isoleucine, valine and leucine are essential amino
acids.
Answer: c
Explanation: Pyruvate gives rise to valine and isoleucine. Glutamate gives rise to glutamine,
arginine and proline. Serine gives rise to glycine and cysteine.
Answer: a
Explanation: Aspartate gives rise to methionine, threonine and lysine. Glutamate gives rise to
glutamine, arginine and proline. Serine gives rise to glycine and cysteine.
Answer: d
Explanation: Leucine is a non-aromatic amino acid.
9. Which of the following can be formed by hydroxylation of phenylalanine?
a) Serine
b) Tyrosine
c) Tryptophan
d) Leucine
View Answer
Answer: b
Explanation: Tyrosine can be formed by hydroxylation of phenylalanine.
Answer:
Explanation: Phosphoribosyl pyrophosphate is a precursor of tryptophan and histidine.
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “Amino
Acids”.
Answer: b
Explanation:
Glycine: H3 N+ – CH2 – COO–
Alanine: H3 N+ – CH(CH3) – COO–
Leucine: H3 N+ – CH(C4 H9) – COO–.
2. The two amino acids having R groups with a negative net charge at pH 7.0 are
a) Aspartate and glutamate
b) Arginine and histidine
c) Cysteine and methionine
d) Proline and valine
View Answer
Answer: a
Explanation:
Aspartate: H3 N+ – CH( CH2 COO– ) – COO–
Glutamate: H3 N+ – CH( C2 H4 COO– ) – COO–.
Answer: b
Explanation: pI = 1⁄2 (pK1 + pK2 ) = 1⁄2 (2.34 + 9.60) = 5.97.
Answer: a
Explanation: Tryptophan and tyrosine are significantly more polar than phenylalanine because of
the tyrosine hydroxyl group and the nitrogen of the tryptophan indole ring.
Answer: a
Explanation: Serine is one of the 11 non-essential amino acids.
Answer: d
Explanation: Phenylalanine is one of the 9 essential amino acids.
7. Which of the following is an imino acid?
a) Alanine
b) Glycine
c) Proline
d) Serine
View Answer
Answer: c
Explanation: Proline is secondary amino acid also called as an imino acid as it contains –C = NH
– OH group.
Answer: a
Explanation: Isoleucine produces both glucose and ketone bodies as an energy source.
9. An amino acid that yields acetoacetyl CoA during the catabolism of its carbon skeleton will be
considered
a) Glycogenic
b) Ketogenic
c) Both glycogenic and ketogenic
d) Essential
View Answer
Answer: b
Explanation: In case of Glycogenic amino acids pyruvate metabolites are formed and in case of
ketogenic amino acids acetoacyl CoA is formed during the catabolism.
Answer: b
Explanation: H5 C2 – C Ḣ (CH3 )- C ̇H(NH2 ) – COOH
The structure clearly shows two chiral centers of isoleucine
Answer: c
Explanation: Kw = [H+ ][OH–] Solving for [OH–] gives
= 7.7 × 10-11 M.
Answer: d
Explanation: Phosphoric acid is triprotic as it can give up three protons
Answer: b
Explanation: The stronger the acid, the lower its pKa. Sulphuric acid is the strongest acid of all
the other acids mentioned, so its pKa is the least.
Answer: a
Explanation: The stronger the base, the higher its pKa. NaOH is the strongest base of all the other
bases mentioned, so its pKa is the highest.
5. The degree of ionization does not depend on?
a) Temperature
b) Current
c) Nature of solvent
d) Concentration
View Answer
Answer: b
Explanation: Degree of ionization is independent of current. It depends only on temperature,
nature of solvent and concentration.
Answer: a
Explanation: CH3 COONa is a salt of weak acid and strong base.
7. K1 and K2 for oxalic acid are 6.5×10-2and 6.1×10-5respectively. What will be the [OH–] in a
0.01M solution of sodium oxalate?
a) 9.6×10-6
b) 1.4×10-1
c) 1.2×10-6
d) 1.3×10-8
View Answer
Answer: c
Explanation: The hydrolysis of C2 O42- is as follows
C2 O42-+ H2 O → HC2O4- + OH–
8. If pKb for fluoride at 25°c is 10.83, the ionization constant of hydrofluoric acid in water at this
temperature is
a) 3.52×10-3
b) 6.75×10-4
c) 5.38×10-2
d) 1.74×10-5
View Answer
Answer: b
Explanation: Kw = Ka × Kb
Ka = Kw / Kb
Ka = 10-14/-log (10.83) = 6.75 × 10-4.
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Answer: c
Explanation: Detergent is a salt of weak acid and strong base.
10. If pH of solution of NaOH is 12.0 the pH of H2 SO4 solution of same molarity will be
a) 2.0
b) 12.0
c) 1.7
d) 10.0387
View Answer
Answer: c
Explanation: pH = 12 then pOH = 2
[OH–] = 10-2
Molarity of NaOH = 10-2
For H2 SO4, molarity = 10-2
[H+] = 2 × 10-2
pH = 2 – log2 = 1.7.
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “Examples
Of Enzymatic actions”.
Answer: c
Explanation: Chymotrypsin enhances the rate of peptide bond hydrolysis by a factor of at least
109.
2. The active site of chymotrypsin consists of a catalytic triad of which of the following amino
acid residues?
a) Serine, histidine and aspartate
b) Serine, histidine and glutamate
c) Threonine, histidine and aspartate
d) Methionine, histidine and aspartate
View Answer
Answer: a
Explanation: Aspartate holds the histidine side chain in the correct direction to accept proton
from serine.
3. Which of the following statements are true about the reactions at the active center of
chymotrypsin?
a) The aspartate residue gives an electron to histidine
b) The aspartate residue gives a proton to histidine
c) The aspartate residue keeps the histidine in the correct direction
d) A proton moves from the aspartate to serine to histidine in the catalytic triad of chymotrypsin
View Answer
Answer: c
Explanation: Aspartate residue accepts a proton from serine.
Answer: c
Explanation: The protein consists of three polypeptide chains linked by disulfide bonds.
Answer: c
Explanation: Chymotrypsin is synthesized in the pancreas.
Answer: b
Explanation: Xylose binds to hexokinase at a position where it cannot be phosphorylated.
Answer: c
Explanation: Enolase catalyzes the reversible degradation of 2-phosphoglycerate to
phosphoenolpyruvate.
Answer: b
Explanation: Hexokinase catalyzes the reversible reaction of β-D-Glucose to glucose 6-
phosphate.
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “The
Covalent Structure of Proteins”.
Answer: b
Explanation: Primary structure of a protein determines how it folds up into a unique three
dimensional structure, which in turn determines the function of a protein.
Answer: c
Explanation: In 1953 James D. Watson and Francis Crick deduced the double-helical structure of
DNA and proposed a structural basis for its precise replication.
Answer: b
Explanation: When we consider amino acid sequence of bovine insulin, the two peptide chains
are joined together by disulfide cross linkages.
Answer: b
Explanation: Ionic interactions, hydrogen and disulfide linkages stabilizes tertiary structure of a
protein.
5. Hemoglobin is a
a) Monomer
b) Dimer
c) Trimer
d) Tetramer
View Answer
Answer:d
It is a tetramer with 2 α chains and 2β chains.
Answer: d
Explanation: The sheet conformation consists of a pair of strands lying side-by-side. The
carbonyl oxygen in one strand hydrogen bond with the amino hydrogen of the adjacent strand.
Answer: d
Explanation: Native state of a protein can be disrupted by temperature, pH, Removal of water
and presence of hydrophobic surfaces.
Answer: c
Explanation: The disulfide bridge formed by oxidation of the sulfhydryl groups on cysteine
stabilizes protein tertiary structure, allowing different parts of the protein chain to be held
together covalently.
Answer: b
Explanation: Hemoglobin is a globular protein and collagen is a fibrous protein.
Answer: a
Explanation: Globular proteins have tertiary structure with hydrophobic amino acid residues and
a surface region of hydrophilic residues; these hydrophobic interactions are responsible for the
folding and shaping of 3° structure of proteins
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on
“Monosaccharides and Disaccharides”.
Answer: a
Explanation: Carbohydrates are dehydrated with con.H2SO4 to form Furfural, which condenses
with anthrone to form a green color.
2. Which of the following are an example of epimers?
a) Glucose & Galactose
b) Glucose & Ribose
c) Mannose & Glucose
d) a & c
View Answer
Answer: a
Explanation: Both glucose and galactose have the same chemical formula but the orientation of –
OH group on C4 molecule in both the compounds are different.
Answer: a
Explanation: Glucuronic acid has free aldehyde group which is responsible for its reducing
property.
4. The red precipitate formed when glucose is heated with “Benedict’s reagent” is
a) Cupric hydroxide
b) Cuprous hydroxide
c) Cupric oxide
d) Cuprous oxide
View Answer
Answer: d
Explanation: When reducing sugars are heated in the presence of an alkali and reduce the Cupric
compounds present in the Benedict’s reagent to cuprous compounds which get precipitated as
insoluble red Cu2O.
Answer: a
Explanation: Selwinoff’s reagent gives positive test for fructose.
Answer: a
Explanation: Galactose is a simple sugar which consists of a single polyhydroxy aldehyde.
Answer: d
Explanation: Maltose is a disaccharide with two monosaccharide glucose units.
Answer: c
Explanation: Maltose contains two D-glucose residues joined by a glycosidic linkage between
C1 of one glucose residue and C4 of the other.
Answer: d
Explanation: Glyceraldehyde is a triose containing 3 carbons.
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on
“Polysaccharides”.
Answer: d
Explanation: Dental plaque formed by bacteria on the surface of teeth is rich in dextrans.
2. In which of the following, glucose residues are linked by β1 &arr; 4 glycosidic bonds?
a) Amylose
b) Starch
c) Cellulose
d) Glycogen
View Answer
Answer: c
Explanation: The glucose residues in cellulose are linked by β1 &arr; 4 glycosidic bonds, in
contrast to the α1 &arr; 4 bonds of amylose, starch and glycogen.
Answer: a
Explanation: Chitin is a linear homopolysaccharide composed of N-acetylglucosamine residues
in β linkage.
4. When all the monosaccharides in a polysaccharide are same type, such type of a
polysaccharide is called a
a) Glycogen
b) Homoglycan
c) Heteroglycan
d) Oligosaccharide
View Answer
Answer: b
Explanation: Homoglycan is a polysaccharide where all the monosaccharides are same type.
Answer: b
Explanation: Starch is the storage form of glucose in plants.
Answer: a
Explanation: Glucose in the form of glycogen is stored in liver and muscles.
Answer: a
Explanation: Starch and glycogen are known as storage polysaccharides.
Answer: c
Explanation: Chitin and cellulose are known as structural polysaccharides.
Answer: b
Explanation: Glycogen is also known as animal starch.
Answer: c
Explanation: Trehalose is a disaccharide.
This set of Biochemistry Questions and Answers for Freshers focuses on “Buffering against pH
changes in Biological Systems”.
Answer: c
Explanation: It is a mixture of weak acid and its salt with strong base.
2. Calculate the pH of a mixture of 0.10M acetic acid and 0.20M sodium acetate. The pKa of
acetic acid is 4.76.
a) 5.1
b) 4.1
c) 6.1
d) 7.1
View Answer
Answer: a
Explanation: pH = pKa + log [acetate]/[acetic acid] = 4.76 + log (0.2/0.1)
= 4.76 + 0.30
= 5.1.
3. Calculate the pKa of lactic acid, given that when the concentration of lactic acid is 0.010M and
the concentration of lactate is 0.087M, the pH is 4.80.
a) 4.0
b) 3.9
c) 3.3
d) 4.1
View Answer
Answer: b
Explanation: pH = pKa + log [lactate]/[lactic acid] pKa = pH – log [lactate]/[lactic acid] = 4.80 –
log (0.087/0.010) = 4.80 – log 8.7
= 3.9.
4. Calculate the ratio of the concentrations of acetate and acetic acid required in a buffer system
of pH 5.30.
a) 3.2
b) 3.3
c) 3.4
d) 3.5
View Answer
Answer: d
Explanation: pH = pKa + log [acetate]/[acetic acid], log [acetate]/[acetic acid] = pH – pKa
= 5.30 – 4.76 = 0.54
[acetate]/ [acetic acid] = antilog 0.54 = 3.5.
Answer: a
Explanation: On dilution pH of buffer solution remains unchanged because the ratio of
concentration of salt and acid (or base) remains unchanged.
Answer: a
Explanation: It is a neutral solution and its pH = 7.
Answer: a
Explanation: An acid buffer is a mixture of weak acid and its salt with strong base, its pH
increases by increasing the concentration of salt.
Answer: a
Explanation: Buffer capacity = number of moles of acid or base added to 1 liter of buffer/change
in pH.
Answer: b
Explanation: Buffer has more capacity when pH = pKa.
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “Water as a
Reactant”.
Answer: b
Explanation: Process A involves absorption of water and B involves double decomposition
reaction.
Answer: d
Explanation: Condensation reaction involves elimination of water molecules.
Answer: a
Explanation: The correct balanced equation is CO2 + H2 O H2 CO3. Carbondioxide reacts with
water to give carbonic acid.
Answer: c
Explanation: Hydrolases, which catalyze hydrolysis reaction involve in food decomposition and
in digestion process.
6. What does it mean when we say that water acts as a “heat buffer”?
a) It keeps the temperature of an organism relatively constant as the temperature of the
surroundings fluctuates.
b) It increases the temperature of an organism as the temperature of the surroundings increases
c) It decreases the temperature of an organism as the temperature of the surroundings increases
d) It increases the temperature of an organism as the temperature of the surroundings decreases
View Answer
Answer: a
Explanation: Water has a high specific heat capacity, it is hard to increase or decrease the water
temperature which requires a lot of heat energy and therefore water acts as a heat buffer.
Answer: c
Explanation: Be is the only alkaline earth metal which does not react with water.
8. What trend does the reactivity of group II elements follow with water?
a) Increases down the group
b) Decreases down the group
c) Does not follow any particular trend
d) No reaction
View Answer
Answer: a
Explanation: As we descend down the group, losing of electrons from the outer orbit of an atom
becomes easy.
9. Which among the following statements is true about the following chemical reaction?
3Fe(s) + 4H2 O → Fe3 O4 (s) + 4H2
a) Iron metal is getting reduced.
b) Water is acting as a reducing agent
c) Water is acting as an oxidizing agent
d) Water is getting oxidized
View Answer
Answer: c
Explanation: Water is getting reduced and it oxidizes iron metal, thus acting as an oxidizing
agent.
Answer: a
Explanation: Ester Hydrolysis
CH3 COOCH3 + H2 O → CH3 COOH + CH3 OH
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “The
Covalent Structure of Proteins”.
Answer: b
Explanation: Primary structure of a protein determines how it folds up into a unique three
dimensional structure, which in turn determines the function of a protein.
2. Who deduced the double-helical structure of DNA?
a) Frederick Sanger
b) Mendel
c) Watson and Francis Crick
d) Anton van Leeuwenhoek
View Answer
Answer: c
Explanation: In 1953 James D. Watson and Francis Crick deduced the double-helical structure of
DNA and proposed a structural basis for its precise replication.
Answer: b
Explanation: When we consider amino acid sequence of bovine insulin, the two peptide chains
are joined together by disulfide cross linkages.
Answer: b
Explanation: Ionic interactions, hydrogen and disulfide linkages stabilizes tertiary structure of a
protein.
5. Hemoglobin is a
a) Monomer
b) Dimer
c) Trimer
d) Tetramer
View Answer
Answer: d
Explanation: The sheet conformation consists of a pair of strands lying side-by-side. The
carbonyl oxygen in one strand hydrogen bond with the amino hydrogen of the adjacent strand.
Answer: d
Explanation: Native state of a protein can be disrupted by temperature, pH, Removal of water
and presence of hydrophobic surfaces.
Answer: c
Explanation: The disulfide bridge formed by oxidation of the sulfhydryl groups on cysteine
stabilizes protein tertiary structure, allowing different parts of the protein chain to be held
together covalently.
Answer: b
Explanation: Hemoglobin is a globular protein and collagen is a fibrous protein.
10. In 3° structure of proteins, folding and shaping is done by
a) Hydrophobic interactions
b) Polar interactions
c) Hydrogen bonding
d) None of the mentioned
View Answer
Answer: a
Explanation: Globular proteins have tertiary structure with hydrophobic amino acid residues and
a surface region of hydrophilic residues; these hydrophobic interactions are responsible for the
folding and shaping of 3° structure of proteins
This set of Biochemistry Multiple Choice Questions & Answers (MCQs) focuses on “Protein
Secondary Structure”.
Answer: d
Explanation: The occurrence of Proline and Glycine residues affect the stability of a α-helix.
Answer: a
Explanation: The hydrophilic / hydrophobic character of amino acid residues is important to
protein tertiary structure rather than to secondary structure. In secondary structure, it is the steric
size of the residues that is important and residues are positioned to minimize interactions
between each other and the peptide chain.
Answer: b
Explanation: Secondary structure of proteins is of two forms α-helix and β-pleated structures.
4. A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same
chain is
a) Primary structure
b) α-helix
c) β-pleated sheets
d) Tertiary structure
View Answer
Answer: b
Explanation: A coiled peptide chain held in place by hydrogen bonding between peptide bonds in
the same chain is α helix.
5. A structure that has hydrogen bonds between polypeptide chains arranged side by side is
a) Primary structure
b) α-helix
c) β-pleated sheets
d) Tertiary structure
View Answer
Answer: c
Explanation: A structure that has hydrogen bonds between polypeptide chains arranged side by
side is β-pleated sheets.
Answer: a
Explanation: Proline and glycine are known as helix breakers as they disrupt the regularity of the
alpha helical backbone conformation.
Answer: c
Explanation: The intramolecular magnetic field around an atom in a molecule changes the
resonance frequency giving structural information about the atom.
Answer: b
Explanation: Less useful in RNA. This is because base pairing is highly conserved than
sequence.
Answer: a
Explanation: Hydrogen bonding is present between the amine hydrogen and carbonyl oxygen
atoms in the peptide backbone.
Answer: d
Explanation: Fibrous structural protein, α-Keratin is α helical