Strategic Analysis and Comprehensive

Question Bank for CUET PG Zoology

(Biochemistry Domain): A Deep Dive into
Syllabus, Trends, and High-Yield
Concepts
1. Introduction: The Evolving Landscape of CUET PG
Zoology
The Common University Entrance Test for Postgraduate Admissions (CUET PG) has
fundamentally restructured the admission ecosystem for Master of Science programs in India.
For aspirants targeting Zoology (Paper Code SCQP28), the examination serves as a critical
gateway to prestigious institutions such as the University of Delhi, Banaras Hindu University,
and Jawaharlal Nehru University. While the overarching discipline is Zoology, the internal
composition of the examination paper reveals a significant reliance on interdisciplinary
subjects, with Biochemistry emerging as a pivotal determinant of candidate success. The
interface between classical zoology and molecular life sciences is where the competitive edge
is often gained or lost.

Biochemistry, within the context of the SCQP28 Zoology paper, is not merely a subset of
questions; it is the foundational logic applied to physiology, developmental biology, and
molecular genetics. The ability to deconstruct metabolic pathways, understand enzyme
kinetics, and visualize molecular structures distinguishes top-tier candidates from the general
cohort. Recent trends observed in the 2022, 2023, and 2024 examination cycles indicate a
decisive shift in the assessment strategy employed by the National Testing Agency (NTA). The
era of rote memorization—where identifying a vitamin deficiency was sufficient—has largely
ceded ground to an era of analytical reasoning. Questions now demand that candidates
correlate structural properties with biological function, interpret experimental data such as
Lineweaver-Burk plots, and predict metabolic outcomes under physiological stress.1

This report provides an exhaustive, expert-level analysis of the Biochemistry component for
CUET PG Zoology. It is structured to serve as a comprehensive strategic document, offering a
forensic analysis of previous years’ difficulty levels, a detailed breakdown of the syllabus as
per NTA guidelines, and, most importantly, a curated bank of 200 high-yield questions. These
questions are not presented in isolation but are embedded within a deep narrative analysis
that explains the underlying theoretical frameworks, common misconceptions, and the
rationale behind the correct answers. This approach ensures that the document serves not
just as a testing tool, but as a robust learning resource comparable to a high-level study
guide.

1.1 Examination Architecture and Difficulty Analysis

The CUET PG Zoology examination (SCQP28) comprises 75 domain-specific questions, a
structure that emphasizes subject matter expertise over general aptitude, following the
removal of Part A in recent iterations for certain universities.3 The weighting of Biochemistry
has historically fluctuated but consistently represents a substantial portion of the paper, often
overlapping with Cell Biology and Physiology.

A longitudinal analysis of the difficulty level from 2022 to 2024 reveals a clear "step-up"
trajectory. The 2022 and 2023 papers were generally categorized as "Moderate to Easy" or
"Moderate," characterized by direct, fact-based questions. For instance, a candidate might
have been asked simply to identify the amino acid with a secondary amino group (Proline).
However, the 2024 cycle marked a departure toward a "Difficult" classification.1 This shift was
driven by the introduction of complex question typologies, including Assertion-Reasoning
(A-R) questions, multi-statement selection questions (e.g., "Choose the correct combination
of statements"), and experimental scenario-based queries.

The implications of this shift are profound. A candidate preparing solely with one-liner facts
would find themselves ill-equipped to handle the nuance of the 2024 paper. For example,
rather than simply asking for the $K_m$ definition, recent questions might present kinetic
data and ask the candidate to infer the type of inhibition or the catalytic efficiency. This report
addresses this gap by ensuring that the 200 selected questions encompass this higher order
of thinking, preparing candidates for the "worst-case" scenario of a highly analytical paper.

1.2 Syllabus Deconstruction and Topic Weightage

The official syllabus for Biochemistry in the CUET PG ecosystem (mapped across SCQP17 and
SCQP28) is vast, yet historical data allows us to identify high-yield clusters.3 The core areas
include:
1.​ Structure and Function of Biomolecules: This includes the detailed chemistry of amino
acids (titration curves, pI calculation), protein structure (Ramachandran plots, secondary
structure stability), carbohydrates (glycosidic linkages, isomers), and lipids (membrane
dynamics).
2.​ Enzymology: Concepts of holoenzymes, apoenzymes, cofactors, and detailed kinetics
(Michaelis-Menten, Lineweaver-Burk, Hanes-Woolf). Inhibition patterns—competitive,
non-competitive, and uncompetitive—are frequently tested using graphical
representations.7
3.​ Bioenergetics and Metabolism: The thermodynamic principles governing biological
systems ($\Delta G$, $\Delta H$, $\Delta S$) and the major catabolic and anabolic
pathways. Glycolysis, the TCA cycle, oxidative phosphorylation, $\beta$-oxidation, and
 the Urea cycle are the pillars of this section. The emphasis is often on the rate-limiting
steps, hormonal regulation, and energetic yield.6
4.​ Biochemical Techniques: Although sometimes categorized under a separate
"Techniques" unit, principles of chromatography (gel filtration, ion exchange),
electrophoresis (SDS-PAGE, IEF), and spectroscopy are integral to the biochemistry
questions found in the Zoology paper.8

The following sections will dissect these topics through the lens of 200 carefully constructed
questions, providing the depth of insight necessary to master the subject.

2. Module I: Amino Acids, Peptides, and Protein

Structure (Questions 1–50)
The study of proteins begins with their monomeric units, the amino acids. In previous years'
papers, questions in this module have ranged from simple structural identification to complex
calculations of isoelectric points (pI). The 2024 pattern suggests a move towards
understanding the physicochemical properties that dictate protein folding and stability.

2.1 Deep Dive: Amino Acid Chemistry and Properties

The following set of questions focuses on the structural uniqueness of the 20 standard amino
acids. A thorough understanding of side-chain chemistry is non-negotiable for the exam.

Table 1: High-Yield Questions on Amino Acid Properties (1–25)

Q. No. Question Text Correct Answer Key

Concept/Rational
e

1 Which amino acid Glycine Glycine has two

lacks a chiral center hydrogen atoms on
and is optically the
inactive? $\alpha$-carbon,
making it achiral.9

2 Which amino acid is Proline The nitrogen in

known as an Proline is part of a
"$\alpha$-helix rigid ring,
breaker" due to its restricting rotation
 cyclic imino and preventing
structure? H-bond
formation.10

3 Identify the amino Methionine Methionine has a

acid that contains a non-reactive sulfur
thioether group in (thioether), unlike
its side chain. Cysteine which has
a reactive thiol
(-SH).

4 Which amino acid Tryptophan Tryptophan has the

absorbs UV light indole ring,
maximally at 280 providing the
nm? highest molar
extinction
coefficient among
aromatics.7

5 At physiological pH Positive (+1) Since pH < pI, the

(7.4), what is the amino group
approximate net accepts a proton,
charge of Lysine (pI resulting in a net
$\approx$ 9.7)? positive charge.11

6 Which amino acid Cysteine Two cysteine

can form disulfide residues oxidize to
bridges, stabilizing form Cystine, a
tertiary structure? covalent disulfide
bond.

7 Which amino acid Tryptophan Tryptophan is

serves as a hydroxylated and
precursor for the decarboxylated to
neurotransmitter form 5-HT
Serotonin? (Serotonin).

8 The imidazole side Histidine Histidine has a pKa

chain of which $\approx$ 6.0,
amino acid allows it allowing it to buffer
to function as a effectively in
 buffer near proteins like
physiological pH? hemoglobin.12

9 Which of the Leucine Part of the "PVT

following is an TIM HALL"
essential amino mnemonic; Leucine
acid for humans? cannot be
synthesized de
novo.9

10 Which amino acid is Tyrosine Tyrosine

both ketogenic and degradation yields
glucogenic? both Fumarate
(glucogenic) and
Acetoacetate
(ketogenic).

11 The "Guanidinium" Arginine This basic group is

group is found in highly basic (pKa
the side chain of: $\approx$ 12.5)
and positively
charged at
physiological pH.7

12 Which amino acid is Citrulline Orithine and

involved in the Urea Citrulline are
cycle as a metabolic
non-proteinogenic intermediates not
intermediate? incorporated into
proteins during
translation.

13 A solution of amino Aspartate Negatively charged

acids separates on amino acids (Asp,
a cation exchange Glu) are repelled by
column. At pH 7.0, the
which amino acid negative/neutral
elutes first? matrix or bind
weakly compared
to positive ones.
14 In the context of pH of zero net The pH where the
acid-base charge zwitterion form
properties, the pI is dominates and
defined as: electrophoretic
mobility is zero.7

15 Which amino acid is Methionine In prokaryotes, it is

encoded by the N-formylmethionin
start codon AUG? e; in eukaryotes, it
is Methionine.

16 Which amino acid Serine Serine, Threonine,

has a hydroxyl and Tyrosine are
group and can the primary targets
undergo for kinases.
phosphorylation?

17 Maple Syrup Urine Branched-chain Leucine, Isoleucine,

Disease (MSUD) is AAs and Valine cannot
caused by be degraded.13
defective
metabolism of:

18 Which amino acid is Arginine NO synthase

the precursor for converts Arginine
Nitric Oxide (NO)? to Citrulline and
NO.

19 Phenylketonuria Tyrosine Deficiency of

(PKU) involves a Phenylalanine
defect in Hydroxylase.
converting
Phenylalanine to:

20 Which amino acid is Glycine Its flexibility allows

often found in the for tight turns in
"turn" regions of the polypeptide
proteins due to its chain.14
small size?
 21 The absorption of Trp, Tyr, Phe The aromatic rings
light by proteins at absorb UV light;
280 nm is primarily Tryptophan
due to: contributes the
most.

22 Which amino acid Proline Unique cyclic

contains a structure
secondary amino connecting the side
group (technically chain to the amino
an imino acid)? nitrogen.

23 Selenocysteine is UGA Normally a stop

encoded by which codon, but context
codon in specific (SECIS element)
contexts? recodes it for
Selenocysteine.

24 Which amino acid is Leucine Leucine and Lysine

non-polar and are the two
purely ketogenic? exclusively
ketogenic amino
acids.

25 The formation of a Condensation Water is eliminated

peptide bond is a when the carboxyl
reaction classified group of one AA
as: reacts with the
amino group of
another.7

Analytical Insight for Module I:

The questions above illustrate the necessity of understanding amino acids beyond their
names. In the 2024 exam, questions may present a hypothetical peptide (e.g.,
"Ala-Gly-Asp-Lys") and ask for its net charge at pH 1, pH 7, and pH 11. Candidates must
understand titration curves. At pH 1, all ionizable groups (N-terminus, C-terminus, side chains)
are protonated. As pH rises, protons dissociate in order of their pKa values ($\alpha$-COOH <
Side chain COOH < $\alpha$-$NH_3^+$ < Side chain $NH_3^+$). The calculation of pI for
amino acids with ionizable side chains involves averaging the pKa values that bracket the
neutral species. For acidic amino acids (Asp, Glu), $pI = (pK_1 + pK_R) / 2$. For basic amino
acids (Lys, Arg, His), $pI = (pK_R + pK_2) / 2$.
2.2 Protein Structure and Stability (Questions 26–50)
Moving up the hierarchy to protein structure, the Ramachandran plot is a perennial favorite in
graduate entrance exams. The plot visualizes the allowed regions of $\phi$ (phi) and $\psi$
(psi) dihedral angles, which are constrained by steric hindrance.

Questions 26–50: Secondary, Tertiary, and Quaternary Structures

26.​In a Ramachandran plot, the values for a right-handed $\alpha$-helix are typically
found in which quadrant?
○​ Analysis: The $\phi$ and $\psi$ angles are both negative ($\approx -57^\circ,
-47^\circ$), placing them in the third quadrant (bottom-left).
27.​Why does Glycine occupy a much larger area on the Ramachandran plot than other
amino acids?
○​ Analysis: Glycine has only a hydrogen atom as a side chain. This lack of steric bulk
allows for a much wider range of $\phi$ and $\psi$ rotations without steric clashes.14
28.​In a $\beta$-pleated sheet, the hydrogen bonds are formed between:
○​ Analysis: The carbonyl oxygen of one peptide bond and the amide hydrogen of a
peptide bond on an adjacent strand (inter-strand bonding), unlike the
$\alpha$-helix which has intra-strand bonding ($n$ to $n+4$).9
29.​Which level of protein structure is preserved when a protein is denatured by urea?
○​ Analysis: Urea disrupts hydrogen bonds and hydrophobic interactions (secondary
and tertiary structure), but the Primary structure (peptide bonds) remains intact.
30.​Collagen is characterized by a triple helix structure. Which repeating sequence is
critical for this?
○​ Analysis: Gly-X-Y, where X is often Proline and Y is Hydroxyproline. Glycine is
required at every third position because it fits into the tight interior of the triple helix.
31.​The "Anfinsen Experiment" demonstrated that:
○​ Analysis: The information required for a protein to fold into its native 3D structure is
contained entirely within its primary amino acid sequence.
32.​Which agent is used to reduce disulfide bonds during SDS-PAGE sample
preparation?
○​ Analysis: $\beta$-Mercaptoethanol (or DTT). This breaks the covalent disulfide
bridges, allowing the protein to unfold completely.15
33.​Quaternary structure refers to:
○​ Analysis: The spatial arrangement of multiple polypeptide subunits (e.g., the
$\alpha_2\beta_2$ tetramer of hemoglobin).
34.​Hemoglobin exhibits cooperative binding of oxygen. This is represented by what
shape of binding curve?
○​ Analysis: Sigmoidal. Myoglobin, which does not show cooperativity, exhibits a
hyperbolic curve.
35.​Which force is primarily responsible for the "Hydrophobic Effect" that drives
protein folding?
○​ Analysis: It is entropy-driven. The aggregation of non-polar groups releases
 ordered water molecules (clathrate cages) into the bulk solvent, increasing the
system's entropy.
36.​Chaperones are proteins that:
○​ Analysis: Assist in the correct folding of other proteins and prevent aggregation of
misfolded intermediates (e.g., HSP70).
37.​The distance per turn (pitch) of a standard $\alpha$-helix is approximately:
○​ Analysis: 5.4 Å (0.54 nm), with 3.6 residues per turn.
38.​Which amino acid is most likely to be found in the interior of a water-soluble
globular protein?
○​ Analysis: Valine (or Leu, Ile, Phe). Hydrophobic residues are buried in the core to
avoid water.9
39.​In an antiparallel $\beta$-sheet, the hydrogen bonds are:
○​ Analysis: Linear (straight) and stronger than in parallel sheets, where the H-bonds
are distorted/angled.
40.​Prion diseases (e.g., Mad Cow Disease) involve a conformational change from:
○​ Analysis: $\alpha$-helix to $\beta$-sheet. The $PrP^{Sc}$ form is rich in
$\beta$-sheets and forms aggregates.
41.​What is the function of the "Zinc Finger" motif?
○​ Analysis: It is a DNA-binding motif found in transcription factors, stabilized by a zinc
ion coordinated by Cys/His residues.
42.​Identify the correct statement regarding Myoglobin.
○​ Analysis: It serves as an oxygen storage protein in muscles, not transport in blood.
43.​Which technique is best for determining the secondary structure content (e.g., %
helix) of a protein?
○​ Analysis: Circular Dichroism (CD) Spectroscopy. $\alpha$-helices show
characteristic negative bands at 208 and 222 nm.15
44.​The "Bohr Effect" in hemoglobin refers to:
○​ Analysis: The decrease in oxygen affinity in response to low pH (high $H^+$) and
high $CO_2$, facilitating oxygen release in tissues.
45.​Which modification targets proteins for degradation by the proteasome?
○​ Analysis: Ubiquitination. A chain of ubiquitin molecules tags the protein for
destruction.
46.​Enzymes that differ in amino acid sequence but catalyze the same reaction are
called:
○​ Analysis: Isozymes (e.g., LDH1 vs LDH5).
47.​The peptide bond has partial double-bond character due to:
○​ Analysis: Resonance between the carbonyl oxygen and the amide nitrogen. This
makes the peptide bond planar and rigid.7
48.​Which of the following is a supersecondary structure (motif)?
○​ Analysis: $\beta$-$\alpha$-$\beta$ unit, Greek key, or Helix-turn-helix.
49.​Calculate the number of peptide bonds in a linear decapeptide.
○​ Analysis: 9. Formula: $n - 1$, where $n$ is the number of residues.
 50.​Domain swapping is a mechanism observed in:
○​ Analysis: Oligomeric proteins, where a domain from one subunit replaces the
corresponding domain in another subunit.

3. Module II: Enzymology and Kinetics (Questions

51–100)
Enzymology is perhaps the most mathematically rigorous section of the Biochemistry
syllabus. PYQs frequently utilize graphs to test a candidate's ability to distinguish between
inhibition types. The questions below cover the Michaelis-Menten model, regulatory
mechanisms, and clinical enzymology.

3.1 Principles of Enzyme Catalysis

Table 2: High-Yield Questions on Enzyme Kinetics (51–75)

Q. No. Question Text Correct Answer Key

Concept/Rational
e

51 Enzymes Activation Energy They lower the

accelerate ($\Delta energy barrier of
reactions primarily G^{\ddagger}$) the transition state;
by modifying which they do not change
thermodynamic $\Delta G$ or
parameter? $K_{eq}$.3

52 In the $$ at $V_{max}/2$ It is the substrate

Michaelis-Menten concentration at
equation, $K_m$ is which the reaction
defined as: rate is
half-maximal.16

53 A low $K_m$ value High Affinity The enzyme

indicates: requires very little
substrate to reach
saturation.7

54 In a $1/V_{max}$ The x-intercept

 Lineweaver-Burk corresponds to
plot, the y-intercept $-1/K_m$.
corresponds to:

55 Competitive $K_m$ increases, The inhibitor

inhibition alters $V_{max}$ same competes for the
kinetic parameters active site, raising
in which way? the apparent
$K_m$, but high $$
can overcome it.17

56 Non-competitive $V_{max}$ The inhibitor binds

inhibition (pure) decreases, $K_m$ to both E and ES
affects kinetics by: same (allosteric site),
removing functional
enzyme from the
pool.7

57 Uncompetitive Both $K_m$ and The inhibitor binds

inhibition is $V_{max}$ only to the ES
characterized by: decrease complex, locking it;
parallel lines on L-B
plot.7

58 What is the $V_{max} / [E_t]$ The number of

turnover number substrate
($k_{cat}$) of an molecules
enzyme? converted to
product per
enzyme molecule
per second.

59 Which parameter is $k_{cat} / K_m$ This ratio accounts

the best measure for both the rate of
of catalytic catalysis and the
efficiency? affinity for the
substrate.16

60 Zymogens are Proteolytic E.g., Trypsinogen is

inactive enzyme cleavage cleaved to Trypsin.
precursors Prevents
 activated by: auto-digestion.

61 An allosteric Sigmoidal Indicates

enzyme (e.g., cooperativity
Hemoglobin/ATCas between subunits.
e) typically yields
which type of
curve?

62 The "Induced Fit" Active site The enzyme

model suggests changes shape conforms to the
that: substrate upon
binding, unlike the
rigid Lock & Key
model.17

63 Which class of Kinases A subclass of

enzymes catalyzes Transferases.
the transfer of a Phosphatases
phosphate group remove phosphate
from ATP? groups.

64 Suicide inhibition is Inhibitor The enzyme

a mechanism covalently binds converts the
where: inhibitor into a
reactive species
that kills the
enzyme (e.g.,
Penicillin).

65 Malonate acts as a Succinate Classic structural

competitive Dehydrogenase analog of
inhibitor for which succinate.9
TCA cycle enzyme?

66 Methotrexate Folic Acid Used in

inhibits chemotherapy to
Dihydrofolate block nucleotide
Reductase (DHFR) synthesis.
by mimicking:
67 Isozymes of Subunit H4 (heart) vs M4
Lactate composition (muscle) tetramers;
Dehydrogenase different affinities
(LDH) differ in: for pyruvate.

68 Ribozymes are: RNA catalysts E.g., the 23S rRNA

peptidyl
transferase activity.

69 Feedback inhibition The committed The first irreversible

usually involves the step step in the pathway
end product to prevent waste.
inhibiting:

70 Which coenzyme is PLP (Vitamin B6) Pyridoxal

required for Phosphate acts as
transamination an electron sink.
reactions?

71 Biotin is a cofactor Carboxylation E.g., Pyruvate

required for which Carboxylase
type of reaction? (adding $CO_2$).7

72 Which ion is often $Mg^{2+}$ Magnesium

required for stabilizes the
ATP-dependent negative charges
enzymatic on the phosphate
reactions? groups of ATP.

73 Which enzyme is Enolase Prevents the

inhibited by conversion of 2-PG
Fluoride in to PEP.9
glycolysis?

74 In the Hanes-Woolf $$ The y-axis

plot, the x-axis represents $/v$;
represents: linear form of MM.

75 An enzyme has a $0.5 V_{max}$ By definition of

$K_m$ of 2 mM. At
 $$ = 2 mM, the $K_m$.
reaction rate $V_0$
will be:

3.2 Advanced Enzymology and Regulation (Questions 76–100)

76.​Aspartate Transcarbamoylase (ATCase) is inhibited by which end product?
○​ Analysis: CTP. This is a classic example of feedback inhibition in pyrimidine
biosynthesis. ATP activates it (balancing purine/pyrimidine).
77.​Which mechanism regulates Glycogen Phosphorylase activity?
○​ Analysis: Covalent Modification (Phosphorylation). Phosphorylase kinase adds a
phosphate to activate it (Phosphorylase a), while phosphatase deactivates it
(Phosphorylase b).
78.​What is the function of the "Oxyanion Hole" in serine proteases like Chymotrypsin?
○​ Analysis: It stabilizes the tetrahedral transition state intermediate by H-bonding
with the negatively charged oxygen.
79.​Trypsin cleaves peptide bonds specifically at the C-terminal side of:
○​ Analysis: Lysine and Arginine. It prefers basic (positively charged) residues.
80.​Chymotrypsin cleaves after:
○​ Analysis: Aromatic residues (Phe, Trp, Tyr). Its specificity pocket is deep and
hydrophobic.
81.​Which vitamin is a precursor for NAD+ and NADP+?
○​ Analysis: Niacin (Vitamin B3). Deficiency leads to Pellagra.9
82.​Thiamine Pyrophosphate (TPP) is a cofactor for:
○​ Analysis: Oxidative Decarboxylation. E.g., Pyruvate Dehydrogenase and
$\alpha$-Ketoglutarate Dehydrogenase.
83.​Which enzyme is the rate-limiting step of Cholesterol biosynthesis?
○​ Analysis: HMG-CoA Reductase. It is the target of Statin drugs.9
84.​Penicillin acts by inhibiting:
○​ Analysis: Glycopeptide Transpeptidase. It prevents bacterial cell wall cross-linking
(suicide inhibition).
85.​The transition state analog is a molecule that:
○​ Analysis: Resembles the transition state of the substrate. Enzymes bind these
analogs much more tightly than the substrate itself.
86.​In multi-substrate reactions, a "Ping-Pong" mechanism implies:
○​ Analysis: One product is released before the second substrate binds. The
enzyme is temporarily modified (e.g., phosphorylated) during the process.
87.​The units of specific activity are:
○​ Analysis: $\mu$mol product / min / mg protein. It is a measure of enzyme purity.
88.​Which enzyme uses a catalytic triad of Ser-His-Asp?
○​ Analysis: Chymotrypsin (and other serine proteases). The triad makes Serine a
potent nucleophile.
89.​What is the effect of temperature on enzyme activity?
 ○​ Analysis: Activity increases with temperature ($Q_{10}$ rule) until the enzyme
denatures, causing a sharp drop.
90.​A competitive inhibitor will cause the Lineweaver-Burk lines to intersect at:
○​ Analysis: The Y-axis. Because $V_{max}$ is unchanged, the intercept ($1/V_{max}$)
is the same.
91.​FAD is derived from which vitamin?
○​ Analysis: Riboflavin (Vitamin B2).9
92.​Which enzyme catalyzes the committed step of Glycolysis?
○​ Analysis: Phosphofructokinase-1 (PFK-1). It is heavily regulated by ATP (inhibitor)
and AMP (activator).
93.​Glucokinase differs from Hexokinase because Glucokinase has:
○​ Analysis: Higher $K_m$ (lower affinity) and is not inhibited by G6P. It acts as a
glucose sensor in the liver.
94.​Which enzyme class involves the cleavage of bonds by means other than
hydrolysis or oxidation?
○​ Analysis: Lyases. E.g., Aldolase cleaves F-1,6-BP.
95.​Coenzyme A contains which vitamin?
○​ Analysis: Pantothenic Acid (Vitamin B5).9
96.​The "Michaelis complex" refers to:
○​ Analysis: The Enzyme-Substrate (ES) complex.
97.​Which molecule acts as a positive allosteric regulator of PFK-1 in the liver?
○​ Analysis: Fructose-2,6-bisphosphate. It overrides ATP inhibition, stimulating
glycolysis.
98.​Lactate Dehydrogenase (LDH) catalyzes a:
○​ Analysis: Redox reaction. Pyruvate is reduced to Lactate; NADH is oxidized to NAD+.
99.​Which metal ion is found in the active site of Carbonic Anhydrase?
○​ Analysis: Zinc ($Zn^{2+}$). It activates a water molecule for catalysis.
100.​ Catalytic antibodies are known as:​
* Analysis: Abzymes. They are antibodies generated against transition state analogs.

4. Module III: Bioenergetics and Metabolism

(Questions 101–160)
This module represents the metabolic core of the Zoology syllabus. The questions span
carbohydrate, lipid, and nitrogen metabolism. The 2024 trend requires candidates to integrate
these pathways—understanding how a defect in one (e.g., ETC) impacts another (e.g., TCA
cycle).

4.1 Carbohydrate Metabolism

101.​ What is the net ATP yield from one molecule of glucose during anaerobic glycolysis?​
 * Analysis: 2 ATP. (4 produced - 2 consumed).
102.​ Which enzyme is unique to Gluconeogenesis and bypasses the Pyruvate Kinase step?​
* Analysis: Pyruvate Carboxylase (Pyruvate $\to$ Oxaloacetate) and PEPCK
(Oxaloacetate $\to$ PEP).9
103.​ Where does the Pentose Phosphate Pathway (HMP Shunt) occur?​
* Analysis: Cytosol. Its main purpose is to generate NADPH and Ribose-5-phosphate.
104.​ Which metabolic pathway is deficient in Von Gierke’s disease?​
* Analysis: Glycogenolysis/Gluconeogenesis. Deficiency of Glucose-6-Phosphatase
prevents the liver from releasing glucose into the blood.
105.​ The Cori Cycle involves the transport of Lactate from:​
* Analysis: Muscle to Liver. The liver converts lactate back to glucose (Gluconeogenesis)
and returns it to the muscle.
106.​ Which enzyme converts Pyruvate to Acetyl-CoA?​
* Analysis: Pyruvate Dehydrogenase Complex (PDH). It occurs in the mitochondrial
matrix.
107.​ Arsenic poisoning inhibits which metabolic step?​
* Analysis: Pyruvate Dehydrogenase and $\alpha$-Ketoglutarate Dehydrogenase.
Arsenite binds to the lipoic acid cofactor.
108.​ Which TCA cycle enzyme is embedded in the inner mitochondrial membrane?​
* Analysis: Succinate Dehydrogenase (Complex II of ETC). All other TCA enzymes are in
the matrix.9
109.​ How many NADH molecules are produced in one turn of the Krebs cycle?​
* Analysis: 3 NADH. (Isocitrate $\to$ $\alpha$-KG; $\alpha$-KG $\to$ Succinyl-CoA;
Malate $\to$ OAA).
110.​ The final electron acceptor in the Electron Transport Chain is:​
* Analysis: Oxygen. It is reduced to water at Complex IV.9
111.​ Which complex of the ETC does NOT pump protons?​
* Analysis: Complex II (Succinate Dehydrogenase). It only passes electrons from FADH2
to CoQ.
112.​ Uncouplers like 2,4-Dinitrophenol (DNP) cause:​
* Analysis: Heat generation without ATP synthesis. They dissipate the proton gradient,
decoupling oxidation from phosphorylation.
113.​ Cyanide blocks electron transport by binding to:​
* Analysis: Complex IV (Cytochrome c Oxidase). It binds to the Heme $a_3-Cu_B$
binuclear center.
114.​ The chemiosmotic theory was proposed by:​
* Analysis: Peter Mitchell. It explains how the proton motive force drives ATP synthesis.
115.​ Which enzyme is responsible for the "Respiratory Burst" in neutrophils?​
* Analysis: NADPH Oxidase. It generates superoxide radicals to kill bacteria.
116.​ Galactosemia is caused by a deficiency in:​
* Analysis: Galactose-1-phosphate uridyltransferase (GALT). Accumulation of
Galactose-1-P is toxic.
117.​ Which enzyme catalyzes the breakdown of Fructose-1,6-bisphosphate?​
 * Analysis: Aldolase A. It splits the 6-carbon sugar into two 3-carbon sugars (DHAP and
GAP).
118.​ The glyoxylate cycle, found in plants and bacteria, allows the conversion of:​
* Analysis: Fats (Acetyl-CoA) to Carbohydrates. Humans lack this pathway and cannot
convert fatty acids to glucose.
119.​ Which molecule serves as the "primer" for glycogen synthesis?​
* Analysis: Glycogenin. It is an enzyme that auto-catalyzes the addition of the first few
glucose residues.
120.​ Insulin stimulates glycolysis by:​
* Analysis: Activating PFK-2, which increases Fructose-2,6-BP levels, thereby activating
PFK-1.

4.2 Lipid Metabolism

121.​ $\beta$-oxidation of fatty acids takes place in the:​
* Analysis: Mitochondrial Matrix.
122.​ Long-chain fatty acids are transported into mitochondria via:​
* Analysis: The Carnitine Shuttle. CPT-I is the regulatory step, inhibited by Malonyl-CoA.9
123.​ The rate-limiting enzyme of Fatty Acid Synthesis is:​
* Analysis: Acetyl-CoA Carboxylase (ACC). It converts Acetyl-CoA to Malonyl-CoA.
124.​ How many ATPs are yielded from the complete oxidation of Palmitate (C16)?​
* Analysis: 106 ATP (Net). (129 gross - 2 for activation). Recent calculations using 2.5/1.5
P/O ratios give 106.
125.​ Ketone bodies are synthesized in the liver from:​
* Analysis: Acetyl-CoA. This occurs when Acetyl-CoA accumulates due to oxaloacetate
depletion (e.g., starvation/diabetes).
126.​ Which of the following is NOT a ketone body?​
* Analysis: Acetyl-CoA. The ketone bodies are Acetone, Acetoacetate, and
$\beta$-Hydroxybutyrate.
127.​ Tay-Sachs disease involves the accumulation of:​
* Analysis: Gangliosides (GM2) due to Hexosaminidase A deficiency.
128.​ Cholesterol is the precursor for:​
* Analysis: Steroid hormones, Vitamin D, and Bile acids.
129.​ Which lipoprotein is responsible for "Reverse Cholesterol Transport"?​
* Analysis: HDL (High-Density Lipoprotein). It carries cholesterol from tissues back to the
liver.
130.​ Fatty acid synthase complex in mammals is:​
* Analysis: A single multifunctional polypeptide dimer. In bacteria, the enzymes are
separate.

4.3 Nitrogen Metabolism and Nucleic Acids

131.​ The first step of the Urea Cycle occurs in:​
* Analysis: Mitochondria. The enzyme CPS-I converts Ammonia and Bicarbonate to
 Carbamoyl Phosphate.
132.​ The immediate precursor for Urea is:​
* Analysis: Arginine. Arginase cleaves Arginine into Urea and Ornithine.
133.​ Alkaptonuria (Black Urine Disease) is a defect in:​
* Analysis: Tyrosine catabolism. Deficiency of Homogentisate Oxidase.
134.​ Lesch-Nyhan syndrome involves a defect in:​
* Analysis: Purine Salvage Pathway. Deficiency of HGPRT leads to uric acid accumulation
(Gout) and self-mutilation.
135.​ The end product of Purine catabolism in humans is:​
* Analysis: Uric Acid. Humans lack Uricase to convert it to Allantoin.
136.​ Which drug inhibits Xanthine Oxidase to treat Gout?​
* Analysis: Allopurinol. It is a suicide inhibitor.
137.​ Glutamate Dehydrogenase catalyzes the conversion of Glutamate to:​
* Analysis: $\alpha$-Ketoglutarate and Ammonia. This is oxidative deamination.
138.​ The carbon atoms of the Pyrimidine ring come from:​
* Analysis: Aspartate and Carbamoyl Phosphate.
139.​ Ribonucleotide Reductase converts:​
* Analysis: Ribonucleotides to Deoxyribonucleotides. It works at the diphosphate level
(NDP $\to$ dNDP).
140.​ Methotrexate inhibits which step in nucleotide synthesis?​
* Analysis: Thymidylate Synthase (indirectly). It inhibits DHFR, depleting the
Tetrahydrofolate required for dUMP $\to$ dTMP conversion.

4.4 High-Yield Metabolism "Rapid Fire" (141–160)

141.​ Signal Transduction: G-proteins bind GTP in the active state and GDP in the inactive
state.
142.​ Cholera Toxin: Permanently activates $G_s\alpha$, leading to high cAMP and
diarrhea.
143.​ Pertussis Toxin: Inhibits $G_i\alpha$, preventing it from lowering cAMP.
144.​ Tyrosine Kinase: The Insulin Receptor is a Receptor Tyrosine Kinase (RTK).
145.​ Vitamin B12 Deficiency: Leads to Methylmalonic Acidemia and Pernicious Anemia.
146.​ Photosynthesis: The Light Reaction occurs in the Thylakoid membrane; Calvin Cycle
in the Stroma.
147.​ Rubisco: The most abundant protein on Earth; fixes $CO_2$.
148.​ C4 Plants: Use PEP Carboxylase to minimize photorespiration (e.g., Maize).
149.​ Glycolysis Regulation: Inhibited by ATP, Citrate; Activated by AMP, F-2,6-BP.
150.​ TCA Regulation: Isocitrate Dehydrogenase is the main control point (activated by
ADP).
151.​ Pyruvate Dehydrogenase: Inhibited by Acetyl-CoA and NADH (Product inhibition).
152.​ Fatty Acid Synthesis: Occurs in the Cytosol.
153.​ Fatty Acid Oxidation: Occurs in the Mitochondria.
154.​ Essential Fatty Acids: Linoleic ($\omega$-6) and $\alpha$-Linolenic ($\omega$-3).
 155.​ Sphingolipids: Backbone is Sphingosine, not Glycerol.
156.​ Surfactant: Dipalmitoylphosphatidylcholine (Lecithin) prevents lung collapse.
157.​ Prostaglandins: Derived from Arachidonic acid via Cyclooxygenase (COX).
158.​ Aspirin: Irreversibly inhibits COX enzymes.
159.​ Ubiquinone (CoQ): Lipid-soluble mobile electron carrier in ETC.
160.​ Cytochrome c: Water-soluble mobile electron carrier in intermembrane space.

5. Module IV: Molecular Biology and Techniques

(Questions 161–200)
This final module bridges Biochemistry with Molecular Biology. Questions here focus on the
"tools of the trade"—how we study biomolecules. The 2024 paper showed a preference for
questions on chromatography principles and DNA topology.
161.​ In Gel Filtration (Size Exclusion) Chromatography, which molecules elute first?​
* Analysis: Large molecules. They are excluded from the porous beads and travel a
shorter path. Small molecules get trapped in the beads.8
162.​ SDS-PAGE separates proteins primarily based on:​
* Analysis: Molecular Weight (Size). SDS coats proteins with a uniform negative charge,
negating charge differences.
163.​ Isoelectric Focusing (IEF) separates proteins based on:​
* Analysis: pI (Isoelectric Point). Proteins migrate in a pH gradient until they reach the pH
equal to their pI.
164.​ The $A_{260}/A_{280}$ ratio is used to determine:​
* Analysis: DNA purity. A ratio of ~1.8 indicates pure DNA; lower values imply protein
contamination.
165.​ Which isotope is commonly used to label DNA backbone phosphates?​
* Analysis: $^{32}P$. $^{35}S$ is used for proteins (Met/Cys).
166.​ What is the function of Dideoxynucleotides (ddNTPs) in Sanger sequencing?​
* Analysis: Chain Termination. They lack the 3'-OH group required for phosphodiester
bond formation.
167.​ In PCR, the annealing temperature is determined by:​
* Analysis: The melting temperature ($T_m$) of the primers. Usually set $5^\circ$C below
$T_m$.
168.​ Restriction Endonucleases belong to which class of enzymes?​
* Analysis: Hydrolases. They hydrolyze the phosphodiester bond.
169.​ Which type of chromatography uses a ligand bound to beads to capture a specific
protein?​
* Analysis: Affinity Chromatography. E.g., Ni-NTA for His-tagged proteins.8
170.​ Northern Blotting is used to detect:​
* Analysis: RNA. Southern is for DNA; Western is for Protein.
171.​ Which enzyme is used to join DNA fragments in cloning?​
 * Analysis: DNA Ligase. It requires ATP (or NAD+ in bacteria) to seal the nick.
172.​ A plasmid vector must contain:​
* Analysis: Origin of Replication (ori), Selectable Marker ($Amp^R$), and Multiple Cloning
Site (MCS).8
173.​ Topoisomerase I relaxes DNA supercoiling by:​
* Analysis: Cutting one strand of the DNA helix. Type II cuts both strands.
174.​ The "Klenow Fragment" of DNA Polymerase I lacks:​
* Analysis: 5' $\to$ 3' Exonuclease activity. It retains polymerase and 3' $\to$ 5'
proofreading activity.
175.​ Which reagent is used to visualize DNA in agarose gels?​
* Analysis: Ethidium Bromide (EtBr). It intercalates between base pairs and fluoresces
under UV.
176.​ The Lac Operon is an example of:​
* Analysis: Negative Inducible system. The repressor binds unless lactose (inducer) is
present.
177.​ Which RNA polymerase synthesizes mRNA in eukaryotes?​
* Analysis: RNA Polymerase II. Pol I makes rRNA; Pol III makes tRNA/5S rRNA.
178.​ What is the function of the Poly-A tail?​
* Analysis: mRNA stability and export. It protects the 3' end from degradation.
179.​ Reverse Transcriptase synthesizes:​
* Analysis: cDNA from an RNA template. Essential for retroviruses and RT-PCR.
180.​ Which technique is used to amplify DNA?​
* Analysis: PCR (Polymerase Chain Reaction).
181.​ Taq Polymerase is used in PCR because:​
* Analysis: It is thermostable. It survives the high denaturation temperatures
($95^\circ$C).
182.​ The "Wobble Hypothesis" explains:​
* Analysis: Degeneracy of the Genetic Code. The 3rd base of the codon pairs less strictly
with the anticodon.
183.​ Which histone is the "Linker" histone?​
* Analysis: H1. H2A, H2B, H3, and H4 form the nucleosome core.
184.​ Euchromatin represents:​
* Analysis: Active, loosely packed chromatin. Heterochromatin is inactive and condensed.
185.​ Telomerase activity is typically high in:​
* Analysis: Stem cells and Cancer cells. It prevents telomere shortening.
186.​ What is a "Transition" mutation?​
* Analysis: Purine $\to$ Purine (A $\leftrightarrow$ G) or Pyrimidine $\to$ Pyrimidine (C
$\leftrightarrow$ T). Transversion is Purine $\leftrightarrow$ Pyrimidine.
187.​ The Shine-Dalgarno sequence is found in:​
* Analysis: Prokaryotic mRNA. It aligns the ribosome for translation initiation.
188.​ What is the role of snRNPs (snurps)?​
* Analysis: Splicing. They form the spliceosome to remove introns.
189.​ Which chemical is used to precipitate DNA?​
 * Analysis: Ethanol (or Isopropanol) with salt.
190.​ Blue-White screening utilizes the gene for:​
* Analysis: $\beta$-Galactosidase (LacZ). Disruption of the gene leads to white colonies
(recombinants).
191.​ ELISA (Enzyme-Linked Immunosorbent Assay) detects:​
* Analysis: Antigens or Antibodies. Uses an enzyme-linked secondary antibody for
colorimetric detection.3
192.​ Monoclonal antibodies are produced by:​
* Analysis: Hybridoma technology. Fusion of B-cells with myeloma cells.
193.​ Which molecule is a second messenger in the Phosphoinositide pathway?​
* Analysis: $IP_3$ and DAG. Generated by PLC cleavage of $PIP_2$.
194.​ The "Fluid Mosaic Model" of the membrane was proposed by:​
* Analysis: Singer and Nicolson (1972).
195.​ Ionophores are molecules that:​
* Analysis: Facilitate ion transport across membranes (e.g., Valinomycin for $K^+$).
196.​ In the intrinsic pathway of apoptosis, which molecule is released from mitochondria?​
* Analysis: Cytochrome c. It binds Apaf-1 to form the apoptosome.
197.​ Caspases are proteases that have which residue at their active site?​
* Analysis: Cysteine. They cleave after Aspartate residues.
198.​ The Rb (Retinoblastoma) protein regulates the cell cycle by inhibiting:​
* Analysis: E2F transcription factors. Phosphorylation of Rb releases E2F, allowing G1
$\to$ S transition.
199.​ p53 is known as the "Guardian of the Genome" because:​
* Analysis: It arrests the cell cycle for DNA repair or induces apoptosis if damage is
irreparable.
200.​ Which blotting technique uses a radiolabeled DNA probe?​
* Analysis: Southern Blot. Used for detecting specific DNA sequences.

6. Strategic Conclusions and Recommendations

The analysis of 200 high-yield questions confirms that the CUET PG Zoology (Biochemistry)
section is no longer a test of superficial recall. The questions cover a spectrum from basic
structural chemistry (Ramachandran plots, Amino acid pI) to complex metabolic integration
(Hormonal regulation, Clinical correlates like PKU/Gout).

Key Takeaways for Aspirants:

1.​ Graph Literacy is Mandatory: You must be able to draw and interpret
Michaelis-Menten, Lineweaver-Burk, and Oxygen dissociation curves.
2.​ Clinical Context: Metabolic pathways are frequently tested in the context of disease
(e.g., enzyme defects). Study pathways with their associated pathologies.
3.​ Technique Precision: Don't just know the names of techniques. Understand the basis of
 separation (Charge vs. Size vs. Affinity) to answer experimental questions.

By mastering these 200 concepts and the underlying theory detailed in the analysis sections,
candidates will be well-positioned to tackle the "Difficult" analytical questions that
characterize the modern CUET PG examination.

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