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Chapter 4 · Class 12 Chemistry

Biomolecules — Important Questions

34 questions With answers CBSE format

SUMMARY: The chapter on Biomolecules in Class 12 Chemistry explores the structure, function, and classification of various biomolecules essential for life processes.
KEY TOPICS: carbohydrates, proteins, enzymes, vitamins, nucleic acids, monosaccharides, disaccharides, polysaccharides, amino acids, DNA and RNA structure

Q1 1 Mark

The simplest aldose (carbohydrate aldehyde) is:

AGlucose
BGlyceraldehyde
CFructose
DSucrose
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Correct answer: Option 2 — Glyceraldehyde
Q2 1 Mark

The bond linking two amino acids in a protein is called:

AGlycosidic bond
BPeptide bond
CPhosphodiester bond
DDisulphide bond
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Correct answer: Option 2 — Peptide bond
Q3 1 Mark

The disaccharide that cannot be hydrolysed to give a reducing sugar pair is:

ASucrose
BMaltose
CLactose
DCellobiose
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Correct answer: Option 1 — Sucrose
Q4 1 Mark

DNA differs from RNA in that DNA contains:

ARibose and uracil
BDeoxyribose and thymine
CUracil and deoxyribose
DRibose and thymine
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Correct answer: Option 2 — Deoxyribose and thymine
Q5 1 Mark

Vitamin C is also known as:

ARetinol
BAscorbic acid
CCalciferol
DNiacin
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Correct answer: Option 2 — Ascorbic acid
Q6 3 Marks

Differentiate between aldoses and ketoses with examples.

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Aldoses: monosaccharides with an aldehyde (-CHO) functional group. Examples: glyceraldehyde (3C), glucose (6C), galactose (6C). Ketoses: monosaccharides with a ketone (>C=O) functional group. Examples: dihydroxyacetone (3C), fructose (6C), ribulose (5C). Both are reducing sugars (in solution they exist in equilibrium with the open-chain form).
Q7 3 Marks

Differentiate between α-amino acids and β-amino acids.

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α-amino acid: the amino group (NH₂) is on the carbon directly adjacent to the carboxyl group (the α-carbon). General formula H₂N-CHR-COOH. The 20 protein-coding amino acids are all α-amino acids. β-amino acid: the amino group is on the second carbon from the carboxyl. β-alanine (NH₂-CH₂-CH₂-COOH) is an example. Only α-amino acids form natural proteins.
Q8 3 Marks

Define isoelectric point of an amino acid.

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The isoelectric point (pI) is the pH at which an amino acid exists predominantly as a zwitterion (no net electrical charge): both COOH is deprotonated to COO⁻ and NH₂ is protonated to NH₃⁺. At pH < pI the molecule is positively charged; at pH > pI it is negatively charged. At pI the molecule has minimum solubility in water and does not migrate in an electric field.
Q9 3 Marks

What are nucleic acids? Name their two types.

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Nucleic acids: long polymers of nucleotides that store and transmit genetic information. Each nucleotide consists of a sugar a phosphate group and a nitrogenous base. Two types: (1) DNA (deoxyribonucleic acid) — contains deoxyribose; bases are A T G C; double-stranded helix; carries hereditary information. (2) RNA (ribonucleic acid) — contains ribose; bases are A U G C; usually single-stranded; involved in protein synthesis (mRNA tRNA rRNA).
Q10 3 Marks

Why are vitamins essential? Distinguish water-soluble from fat-soluble vitamins.

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Vitamins are organic compounds required in trace amounts for normal metabolism but not synthesised by the body — must be obtained from diet. Water-soluble vitamins: B-complex (B1 B2 B6 B12 etc) and C (ascorbic acid). Excreted in urine; not stored; must be consumed regularly. Fat-soluble vitamins: A D E K. Stored in liver and adipose tissue; deficiency develops slowly; excess can cause toxicity (especially A and D).
Q11 6 Marks

Discuss the structures and biological importance of glucose.

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Open-chain structure: glucose is an aldohexose (CHO-CHOH-CHOH-CHOH-CHOH-CH₂OH) with 4 chiral centres. D-glucose is the natural form. Cyclic structures: in solution glucose exists predominantly (>99%) as a 6-membered ring (pyranose form) formed by reaction of C5-OH with C1-CHO. Two anomers — α (OH at C1 below ring) and β (OH at C1 above ring) — exist in equilibrium (mutarotation). Biological importance: primary energy source (glycolysis krebs cycle); building block of starch glycogen and cellulose; blood sugar maintained by insulin/glucagon balance.
Q12 6 Marks

Explain the four levels of protein structure.

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Primary: linear sequence of amino acids linked by peptide bonds. Determines all higher structure. Secondary: local folding patterns stabilised by hydrogen bonds — α-helix (right-handed coil) and β-pleated sheet are most common. Tertiary: overall 3D fold of the entire chain stabilised by R-group interactions: H-bonds salt bridges hydrophobic interactions disulphide bridges. Quaternary: assembly of two or more polypeptide chains (subunits) into a functional protein. Examples: haemoglobin (4 chains 2α 2β); insulin (2 chains linked by S-S bonds).
Q13 6 Marks

Differentiate between starch and cellulose.

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Starch: storage polysaccharide in plants. Two components: amylose (linear α(1→4) glucose linkages 20%) and amylopectin (branched α(1→4) and α(1→6) 80%). Hydrolysed by α-amylase in saliva and pancreas. Provides energy. Cellulose: structural polysaccharide of plant cell walls. Linear β(1→4) glucose linkages with extensive hydrogen bonding between chains forming microfibrils. Insoluble. Cannot be digested by humans (no β-glucosidase) but ruminants and termites use bacterial cellulose. The α vs β linkage difference radically changes properties.
Q14 6 Marks

Discuss the structure and function of DNA double helix.

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Watson and Crick (1953) proposed the double-helix model. Two antiparallel polynucleotide chains wound around each other in a right-handed helix. Sugar-phosphate backbone on outside; bases (A T G C) inside paired by H-bonds (A=T two bonds; G≡C three bonds — Chargaff rule). One full turn = 3.4 nm = 10 base pairs. Bases stacked at 0.34 nm apart. Function: stores genetic information in the sequence of bases; replication via semi-conservative mechanism (each strand serves as template); transcription to mRNA; translation to protein at ribosome. The double helix's stability and information-encoding capacity make it the molecular basis of heredity.
Q15 6 Marks

Discuss the role of enzymes as biological catalysts.

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Enzymes are protein (sometimes RNA) catalysts that accelerate biochemical reactions. Properties: (1) High specificity — usually one enzyme one reaction (lock-and-key or induced-fit model). (2) Operate at mild conditions (body T pH 7). (3) Lower activation energy by stabilising the transition state. (4) Not consumed in reaction. (5) Activity regulated by inhibitors activators allosteric effectors and by post-translational modification. Examples: amylase digests starch; pepsin and trypsin digest proteins; ATP synthase makes ATP. Each enzyme has an optimum T and pH; deviation reduces activity.
Q16 6 Marks

Differentiate between glucose and fructose in tabular form on five features.

Q17 1 Mark

Assertion (A): Glucose exists predominantly in cyclic form in solution.

Reason (R): The aldehyde group of glucose reacts intramolecularly with the C5 OH forming a 6-membered hemiacetal ring (pyranose form).

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Correct answer: Option 1 — Both A and R are true, and R is the correct explanation of A.
Q18 1 Mark

Assertion (A): Sucrose is a non-reducing sugar.

Reason (R): The glycosidic bond in sucrose is formed between the anomeric carbons of glucose and fructose blocking both potential reducing sites.

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Correct answer: Option 1 — Both A and R are true, and R is the correct explanation of A.
Q19 1 Mark

Assertion (A): The sequence of amino acids determines the protein's 3D structure.

Reason (R): The R-group interactions encoded in the primary sequence drive folding into the unique tertiary structure.

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Correct answer: Option 1 — Both A and R are true, and R is the correct explanation of A.
Q20 1 Mark

Assertion (A): DNA replication is semi-conservative.

Reason (R): Each daughter DNA molecule contains one parental strand and one newly synthesized strand.

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Correct answer: Option 1 — Both A and R are true, and R is the correct explanation of A.
Q21 1 Mark

Assertion (A): Essential amino acids must be obtained from diet.

Reason (R): The human body cannot synthesise these amino acids (e.g. lysine tryptophan) at sufficient rates so dietary intake is required.

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Correct answer: Option 1 — Both A and R are true, and R is the correct explanation of A.
Q22 1 Mark

Statement 1: Glucose is an aldohexose.

Statement 2: Fructose is a ketohexose.

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Correct answer: Option 1 — Both statements are true.
Q23 1 Mark

Statement 1: Sucrose hydrolyses to glucose and fructose.

Statement 2: Maltose hydrolyses to two molecules of glucose.

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Correct answer: Option 1 — Both statements are true.
Q24 1 Mark

Statement 1: All α-amino acids (except glycine) are chiral.

Statement 2: Natural amino acids in proteins have the L configuration.

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Correct answer: Option 1 — Both statements are true.
Q25 1 Mark

Statement 1: DNA contains deoxyribose; RNA contains ribose.

Statement 2: DNA contains the base thymine; RNA contains the base uracil.

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Correct answer: Option 1 — Both statements are true.
Q26 1 Mark

Statement 1: Enzymes are highly specific biological catalysts.

Statement 2: Enzymes have an active site that binds the substrate and stabilises the transition state.

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Correct answer: Option 1 — Both statements are true.
Q27 3 Marks
In aqueous solution glucose exists as an equilibrium mixture of α-D-glucose (~36%) β-D-glucose (~64%) and a small fraction (<1%) of the open-chain form. Each anomer has a specific optical rotation: α gives +112° β gives +19°. The equilibrium results in an observed rotation of ~+52° — known as mutarotation.
  1. Glucose in aqueous solution exists as:
    AOpen-chain only
    BCyclic only
    CEquilibrium between cyclic and open-chain forms
    DNo equilibrium
  2. The dominant form of glucose in solution is the:
    APyranose
    BFuranose
    COpen chain
    DAll three
  3. Why is the β-anomer of glucose slightly more stable than the α-anomer?
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1. Option 3 — Equilibrium between cyclic and open-chain forms
2. Option 1 — Pyranose
3. Pure α-D-glucose (specific rotation +112°) when dissolved in water slowly changes its rotation to a steady value of +52°. The same final value is obtained starting from pure β-D-glucose (initial +19°). This phenomenon — mutarotation — is explained by interconversion of α and β anomers via the open-chain form: ring opens at C1 inverts at C1 and re-forms with either α or β configuration. Equilibrium fraction of each anomer is determined by relative thermodynamic stability (β has equatorial OH at C1 — slightly more stable).
Q28 3 Marks
Insulin a small protein has 51 amino acid residues arranged in two polypeptide chains: A chain (21 residues) and B chain (30 residues) linked by disulphide bridges. The primary structure (the linear sequence) determines all higher levels of structure and the biological function.
  1. Primary structure is the:
    ALinear sequence of amino acids
    B3D folding pattern
    CQuaternary structure
    DDisulphide bridges
  2. The bonds linking adjacent amino acids in the chain are:
    APeptide bonds
    BHydrogen bonds
    CDisulphide bonds
    DHydrophobic interactions
  3. Identify the type of bond joining the A and B chains in insulin.
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1. Option 1 — Linear sequence of amino acids
2. Option 1 — Peptide bonds
3. Primary structure: the linear sequence of amino acids linked by peptide (-CO-NH-) bonds. Secondary structure: local folding patterns (α-helix β-sheet) stabilised by H-bonds along the backbone. Tertiary structure: overall 3D fold of the entire chain stabilised by R-group interactions (disulphide bridges H-bonds salt bridges hydrophobic). Quaternary structure: assembly of multiple polypeptide chains. Insulin's quaternary structure (two chains A + B) is critical for activity. The primary sequence determines folding and ultimately function — change a single key residue and the protein may misfold.
Q29 3 Marks
In 1958 Meselson and Stahl demonstrated that DNA replication is semi-conservative: each daughter DNA molecule contains one parental strand and one newly synthesised strand. They used ¹⁵N labelling and density-gradient centrifugation to distinguish parental and daughter DNA.
  1. DNA replication is:
    AConservative
    BSemi-conservative
    CDispersive
    DRandom
  2. The semi-conservative nature was demonstrated by:
    AWatson and Crick
    BMeselson and Stahl
    CChargaff
    DPauling
  3. Why was the semi-conservative model strongly supported but not the conservative model?
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1. Option 2 — Semi-conservative
2. Option 2 — Meselson and Stahl
3. Three models had been proposed: (1) Conservative — both daughter molecules either contain only old or only new DNA. (2) Semi-conservative — each daughter has one old and one new strand. (3) Dispersive — old and new are mixed within each strand. Meselson-Stahl used ¹⁵N (heavy isotope) to label parental DNA then transferred to ¹⁴N medium. After one generation all DNA was hybrid (one ¹⁵N strand + one ¹⁴N strand) — confirming the semi-conservative model. After two generations 50% hybrid + 50% all-light DNA. The experiment is one of the most elegant in biology.
Q30 3 Marks

Study common biomolecules and their building blocks:

BiomoleculeBuilding blockLinkageFunction
CarbohydratesMonosaccharides (glucose fructose etc.)Glycosidic bondEnergy storage / structural
ProteinsAmino acidsPeptide bondCatalysis structure transport
LipidsFatty acids + glycerolEster bondEnergy storage / membranes
Nucleic acidsNucleotides (sugar + phosphate + base)Phosphodiester bondInformation storage and transfer
  1. The bond between two amino acids in a protein is the:
    AGlycosidic
    BPeptide
    CPhosphodiester
    DEster
  2. The bond between two nucleotides in DNA is the:
    AGlycosidic
    BPeptide
    CPhosphodiester
    DEster
  3. Identify the bond type in a triglyceride and explain why fats are hydrophobic.
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1. Option 2 — Peptide
2. Option 3 — Phosphodiester
3. Each class of biomolecule has a characteristic linkage between its monomers. Carbohydrates (sugars) link via glycosidic bonds — formed by condensation between OH groups. Proteins link amino acids via peptide bonds — formed between COOH and NH₂ with loss of water. Lipids (triglycerides) link fatty acids to glycerol via ester bonds. Nucleic acids link nucleotides via phosphodiester bonds — phosphate bridges between sugars. The linkage type determines the chemistry of digestion and the conditions for synthesis in the lab.
Q31 3 Marks

Study the structures of nucleic acid bases:

BaseTypeFound in DNAFound in RNA
Adenine (A)PurineYesYes
Guanine (G)PurineYesYes
Cytosine (C)PyrimidineYesYes
Thymine (T)PyrimidineYesNo
Uracil (U)PyrimidineNoYes
  1. The base unique to RNA (not in DNA) is:
    AThymine
    BUracil
    CCytosine
    DAdenine
  2. Watson-Crick base pairing in DNA links:
    AA and T
    BA and U
    CG and C
    DA and G
  3. Why is T preferred over U in DNA but U is used in RNA?
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1. Option 2 — Uracil
2. Option 1 — A and T
3. DNA bases: A T G C. RNA bases: A U G C (T is replaced by U). Purines (A G) have a fused two-ring structure. Pyrimidines (C T U) have a single-ring structure. Watson-Crick pairing in DNA: A=T (2 H-bonds) G≡C (3 H-bonds). In RNA A pairs with U instead. Chargaff's rule: amount of A = amount of T; amount of G = amount of C — supporting base-pairing. The pyrimidine T has a methyl group that U lacks — making T more chemically stable and thus suitable for long-term storage in DNA.
Q32 6 Marks

Identify the building block (monomer) of each biomolecule and the type of linkage between monomers.

BiomoleculeBuilding blockLinkage
Carbohydrates??
Proteins??
Lipids (triglycerides)??
Nucleic acids??
Starch??
Cellulose??
Q33 6 Marks

Compare the structural and functional properties of DNA and RNA.

PropertyDNARNA
Sugar??
Bases??
Strand structure??
Function??
Q34 3 Marks

Study the Watson-Crick base pairing diagram and answer:

Biomolecules figure
  1. Adenine pairs with thymine through:
    AOne H-bond
    BTwo H-bonds
    CThree H-bonds
    DNo H-bonds
  2. The stronger base pair (more H-bonds) is:
    AA=T
    BG≡C
    CBoth equally
    DA=G
  3. State Chargaff's rule and explain how complementary base pairing enables accurate DNA replication.
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1. Option 2 — Two H-bonds
2. Option 2 — G≡C
3. Watson and Crick (1953) proposed the double-helix model of DNA. The two strands are antiparallel and held together by specific base pairing: adenine (A, purine) pairs with thymine (T, pyrimidine) via TWO hydrogen bonds; guanine (G, purine) pairs with cytosine (C, pyrimidine) via THREE hydrogen bonds. This complementary pairing is the basis of Chargaff's rule: in any DNA, the amount of A equals T, and the amount of G equals C. The G≡C pair is stronger, so DNA regions rich in G/C are more thermally stable. The specificity of base pairing is what allows accurate DNA replication: each strand serves as a template for the complementary new strand.

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