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Chemistry — Class 12 — L29: Biomolecules

NIOS Code 313 · Module 7 · Chemistry of Organic Compounds

Notes extracted from NIOS Chemistry Course (313), Lesson 29 — Biomolecules (313_Chemistry_Eng_Lesson29.pdf). Content covers sections 29.1–29.7.
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Overview — Molecules of Life

Living organisms are built and maintained by complex organic biomolecules: carbohydrates, proteins, lipids, nucleic acids, enzymes, hormones and vitamins. This lesson covers their classification, key structural features and biological roles — high-yield for boards and foundation for biochemistry.

Section 1: Carbohydrates (29.1)

Produced in plants by photosynthesis. Chemically: polyhydroxy aldehydes or ketones, or substances that yield them on hydrolysis. Sweet monosaccharides/disaccharides are sugars; table sugar is sucrose.

Classification by hydrolysis:

  • Monosaccharides — cannot hydrolyse further (glucose, fructose, ribose). Aldose (–CHO) or ketose (C=O); named by carbon count (aldohexose, ketohexose, etc.).
  • Disaccharides — two monos (sucrose, maltose, lactose).
  • Oligosaccharides — 2–10 monos units.
  • Polysaccharides — many units (starch, cellulose, glycogen).

D/L configuration: related to glyceraldehyde. If the lowest asymmetric carbon matches D-(+)-glyceraldehyde (–OH on the right in Fischer projection), the sugar is D-; otherwise L-. Natural glucose is D-glucose.

Important monos: D-glucose (aldohexose, most abundant organic compound); D-fructose (ketohexose, fruit/honey); D-ribose (RNA); 2-deoxy-D-ribose (DNA, no OH at C-2).

In nature, monosaccharides exist mainly as cyclic hemiacetals. Glucose forms a six-membered ring; α and β forms differ only at C-1 — these are anomers. Ribose forms a five-membered ring (α/β).

Carbohydrate Ladder Monoglucose Disucrose Polystarch Cellulosestructure Hydrolysis count defines the class
Mono → di → poly — based on hydrolysis behaviour.
2 mono − H₂O → disaccharide (glycoside link)
Condensation joins rings · reverse = hydrolysis

Disaccharides: joined by a glycoside linkage (loss of water between OH groups). Maltose = two α-glucose; sucrose = glucose + fructose; lactose (milk sugar) = glucose + galactose.

Polysaccharides: starch (plant storage) = amylose (linear α-D-glucose, water-soluble fraction) + amylopectin (branched, insoluble). Cellulose (wood, plant walls) = long chains of β-D-glucose — humans lack enzymes to digest it. Glycogen = animal storage polymer of α-D-glucose, more branched than amylopectin.

Biological roles: energy storage (starch/glycogen); structure (cellulose); ribose/deoxyribose in nucleic acids; glycoproteins and glycolipids for recognition.

Storage vs Structure α-Glucose polymersstarch · glycogen β-Glucose polymercellulose (structure) Same monomer · different linkage · different role
α for digestible storage · β for plant fibre.

Section 2: Proteins (29.2)

Most abundant macromolecules in cells; name from Greek proteios (“of prime importance”). Polymers of α-amino acids. Diet sources: pulses, eggs, meat, milk.

Simple proteins hydrolyse to amino acids only. Fibrous: insoluble, thread-like (collagen, elastin, keratin). Globular: folded spheres, often soluble (egg albumin, serum globulin, haemoglobin).

Conjugated proteins also yield a non-amino prosthetic group: nucleo-, glyco-, chromo-, lipo-, metallo-, phosphoproteins.

By function: transport (Hb, lipoproteins); storage (casein, ovalbumin); structural (keratin, collagen); defence (antibodies); enzymes (pepsin, trypsin); regulatory (insulin).

α-Amino acids: H₂N–CH(R)–COOH. About 20 in proteins; all L-configuration. ~10 are essential (must come from diet).

Peptide bond: –COOH of one AA + –NH₂ of another → amide –CO–NH– + H₂O. Dipeptide, tripeptide… polypeptides; proteins are large polypeptides (insulin has 51 AA but is called a protein). Write sequences with N-terminal (free NH₂) on the left and C-terminal (free COOH) on the right.

AA₁ + AA₂ → dipeptide (−H₂O) · –CO–NH– peptide bond
Amide link · backbone of all proteins

Structural levels:

  • Primary: amino-acid sequence — decides function.
  • Secondary: regular H-bonding of backbone → α-helix or β-pleated sheet.
  • Tertiary: overall 3D fold (e.g. myoglobin).
  • Quaternary: assembly of multiple polypeptide chains (e.g. haemoglobin subunits).

Denaturation: heat or pH change breaks H-bonds; helices uncoil, globules unfold — curdling of milk (lactic acid), cooking egg white. Some proteins (skin, nails, stomach lining) resist denaturation.

Roles: cell structure; enzymes; immunoglobulins; hormones (insulin); growth/repair; fibrinogen (clotting); haemoglobin transports O₂.

Protein Structure Levels 1° sequence 2° helix/sheet 3° fold 4° multi Sequence → H-bonds → 3D → complexes
Four levels — exam staple.

Section 3: Lipids (29.3)

From Greek lipos (fat). Cell constituents insoluble in water, soluble in low-polarity solvents (ether, chloroform, benzene).

Simple lipids: esters → fatty acids + alcohol on hydrolysis. Fats, oils, waxes.

Compound lipids: also phosphoric acid, sugars or proteins (phospholipids, glycolipids).

Derived lipids: metabolic products such as steroids and fat-soluble vitamins.

Triglycerides: glycerol esterified with three long-chain fatty acids (often C₁₂–C₂₆). Hydrolysis → glycerol + 3 fatty acids. Fat = solid/semisolid at room temperature; oil = liquid. Saturated chains raise melting point (fats); unsaturation lowers it (oils). Catalytic hydrogenation saturates double bonds — oil → fat (vanaspati ghee). Body stores excess carbohydrate energy as fat; plant oils often in seeds.

Waxes: esters of fatty acids with long monohydric alcohols (C₂₆–C₃₄); protective coatings (beeswax: myricyl palmitate). Not the same as paraffin wax (hydrocarbons).

Phospholipids: membrane building blocks. Steroids: characteristic ring system; cholesterol widely distributed; backbone of many hormones. Fat-soluble vitamins A, D, E, K are derived lipids.

Importance: energy store; aid absorption of ADEK; insulation; membranes; steroid signalling; some enzymes need lipids.

triglyceride + 3H₂O → glycerol + 3 RCOOH  |  oil + H₂ → fat
Hydrolysis frees fatty acids · hydrogenation hardens oils
Fat vs Oil Fatsolid RT · more saturated Oilliquid RT · more unsaturated Same triglyceride class · physical state differs
Room-temperature state defines fat vs oil.

Section 4: Nucleic Acids (29.4)

Chromosomes carry heredity; chemically they are nucleic acids — acidic polymers from the cell nucleus. Two types: DNA and RNA.

Polymers of nucleotides. Each nucleotide = nitrogenous base + pentose sugar + phosphoric acid. Chain: sugar–phosphate backbone with bases as side groups.

DNA: sugar = 2-deoxyribose; bases adenine (A), guanine (G), cytosine (C), thymine (T). Double helix (Watson & Crick, 1953): two complementary strands held by H-bonds — A pairs with T, G with C. Sequence of bases = primary structure; double helix = secondary structure.

RNA: sugar = ribose; bases A, G, C and uracil (U) instead of T. Usually single-stranded (may fold). Types: mRNA (message), rRNA (ribosome), tRNA (amino-acid carrier).

Replication: strands unwind; each templates a new complementary strand → two identical double helices (each with one old + one new strand).

Protein synthesis: DNA code → mRNA → cytoplasm; tRNA brings amino acids; peptide bonds form. DNA stores the code; RNA executes synthesis.

nucleotide = base + sugar + phosphate  |  A–T · G–C
Building block of DNA/RNA · complementary base pairing
DNA vs RNA DNAdeoxyribose · A G C Tdouble helix · code RNAribose · A G C Uusually single · synthesis T in DNA · U in RNA
Core structural and functional differences.

Section 5: Enzymes (29.5)

Biochemical catalysts that allow complex reactions at body temperature (~310 K), e.g. digestion. Almost all are globular proteins. Named with ending -ase (maltase hydrolyses maltose; esterase acts on esters).

Mechanism: lower activation energy. Lock-and-key: substrate binds active site → enzyme–substrate complex → products + free enzyme. Highly specific; needed in tiny amounts; work in dilute aqueous solution at moderate T and specific pH. Many need coenzymes (non-protein partners, e.g. NAD for dehydrogenases). Many vitamins act as coenzyme precursors.

E + S ⇌ ES → E + P
Lock-and-key · catalyst regenerated

Section 6: Hormones (29.6)

Chemical messengers from endocrine glands via blood to target tissues.

Steroid hormones: sex hormones (androgens: testosterone; estrogens: estradiol; progesterone for pregnancy) and adrenocortical hormones (aldosterone — Na⁺/K⁺ balance; hydrocortisone — glucose metabolism, inflammation).

Peptide hormones: oxytocin (uterine contraction in childbirth); vasopressin (blood pressure); insulin (pancreas — glucose metabolism; deficiency → diabetes mellitus).

Section 7: Vitamins (29.7)

Small organic molecules required in the diet in trace amounts for growth and metabolism. Many function as coenzymes.

Water-soluble: vitamin C (ascorbic acid — bleeding gums); B₁ thiamin (fatigue); B₂ riboflavin (cracked lips); B₆ (anemia); niacin (dermatitis, dementia); folic acid; B₁₂ (anemia, neuro issues); pantothenic acid; biotin.

Fat-soluble: A (night blindness, dry skin); D (rickets, osteomalacia); E (RBC hemolysis); K (bleeding, delayed clotting).

Remember: fat-soluble ADEK need dietary fat for absorption; water-soluble excess is more easily excreted.

Vitamin Solubility Water-solubleC · B-complex Fat-solubleA · D · E · K Match vitamin to deficiency symptom in exams
Two solubility classes — different storage and absorption.

Exam Connections and Chapter Summary

High-yield: carb classification and glycoside link; α vs β polymers; peptide bond and 1°–4° protein structure; denaturation; fat vs oil; nucleotide parts; DNA/RNA differences and base pairing; enzyme lock-and-key; insulin and diabetes; vitamin deficiency table (especially A, C, D, K, B₁₂).

Links L28 (amino groups, peptides) and L27 (carbonyls in sugars). Next module topic in the course list: soaps, detergents and polymers (L31). Practice short definitions and comparison tables — they score reliably.

MCQ Quiz — L29 Biomolecules

0 / 10 correct

Flashcards — L29

1 / 18

Golden Rules — L29 Biomolecules

Most exam-important points from this chapter:

Carbohydrates

Polyhydroxy carbonyls. Mono/di/poly. Glycoside link. α-starch/glycogen · β-cellulose. D/L from glyceraldehyde.

Proteins

α-AA · peptide bond · 1°–4° structure. Essential AA in diet. Fibrous/globular/conjugated. Denaturation by heat/pH.

Lipids

Water-insoluble. Triglycerides: fat solid, oil liquid. Hydrogenation. Phospholipids, steroids, ADEK.

Nucleic acids

Nucleotide units. DNA: deoxyribose, T, double helix, A–T/G–C. RNA: ribose, U, protein synthesis.

Enzymes & vitamins

Enzymes: protein, specific, lock-key, mild conditions. Vitamins: water vs fat soluble; match deficiencies.

Mono · di · poly saccharides
α / β anomers · glycoside
Starch · cellulose · glycogen
α-Amino acids · peptide bond
1° · 2° · 3° · 4° structure
Fat vs oil · triglyceride
DNA · RNA · base pairs
Enzyme lock-and-key
Vitamins A–K · hormones

Section 1: Carbohydrates

NIOS Chemistry 313, Module 7 — Biomolecules (sections 29.1–29.7).

Definition & Classification

Polyhydroxy aldehydes/ketones or substances that give them on hydrolysis

Mono: cannot hydrolyse further (glucose, fructose) · aldose/ketose + carbon count

Di: 2 monos (sucrose, maltose, lactose) · Oligo: 2–10 · Poly: many (starch, cellulose, glycogen)

Key Structures

D/L from glyceraldehyde · lowest asymmetric C · D-glucose most abundant

Cyclic hemiacetal · α/β anomers at C-1 · glycoside linkage joins monos

Sucrose = glucose + fructose · maltose = 2× α-glucose · lactose = glucose + galactose

Starch: amylose (linear α) + amylopectin (branched α) · cellulose: β-glucose · glycogen: animal storage (more branched)

Section 2: Proteins

Amino Acids & Structure Levels

α-Amino acid: H₂N–CH(R)–COOH · ~20 in proteins · all L · ~10 essential (diet)

Peptide bond: –CO–NH– · N-terminal left, C-terminal right

1°: sequence · 2°: α-helix / β-sheet (H-bonds) · 3°: 3D fold · 4°: multi-chain assembly

Fibrous (insoluble: keratin, collagen) · globular (soluble: albumin, Hb) · conjugated + prosthetic group

Denaturation: heat/pH break H-bonds → unfold (egg white, curdling)

Section 3: Lipids

Types & Fats vs Oils

Water-insoluble · soluble in nonpolar solvents · simple / compound / derived

Triglyceride = glycerol + 3 fatty acids · fat solid RT · oil liquid RT

Saturated → higher m.p. (fats) · unsaturated → oils · hydrogenation → vanaspati

Waxes: long monohydric alcohol esters · phospholipids · steroids (cholesterol) · fat-sol vitamins A,D,E,K

Section 4: Nucleic Acids, Enzymes, Hormones, Vitamins

DNA / RNA

Nucleotide = base + pentose + phosphate · polynucleotide chain

DNA sugar = 2-deoxyribose · bases A,G,C,T · double helix · A–T · G–C

RNA sugar = ribose · bases A,G,C,U · usually single strand · mRNA, rRNA, tRNA

DNA: replication + code · RNA: protein synthesis

Enzymes · Hormones · Vitamins

Enzymes: protein biocatalysts · lock-and-key · specific · -ase · coenzymes

Hormones: endocrine messengers · steroids (sex, adrenal) · peptides (insulin, oxytocin, vasopressin)

Vitamins: dietary, trace · water-sol (C, B-complex) · fat-sol (A,D,E,K) · deficiency diseases

Section 5: Definitions

Anomer: Cyclic sugar isomers differing only at the hemiacetal carbon (C-1 in glucose).

Peptide bond: Amide link between α-COOH of one amino acid and α-NH₂ of another.

Essential amino acids: Cannot be synthesised by body; required in diet (~10).

Nucleotide: Nitrogen base + pentose sugar + phosphoric acid unit.

Denaturation: Loss of native protein structure by heat, pH, etc. (H-bonds disrupted).

Section 6: Visual Map

L29 Map — Biomolecules Sugars Proteins Lipids DNA/RNA Enzymes catalyse · hormones signal · vitamins cofactors · diet building blocks A–T / G–C · peptide bond · fat solid / oil liquid · lock-and-key

Section 7: Q&A (12 Questions)

Q1: Chemical definition of carbohydrate?

Polyhydroxy aldehyde or ketone, or substance that yields these on hydrolysis.

Q2: Hydrolysis products of sucrose?

Glucose + fructose.

Q3: Starch vs cellulose monomer linkage?

Starch: α-D-glucose · cellulose: β-D-glucose (humans lack cellulase).

Q4: What is a peptide bond?

Amide –CO–NH– between two α-amino acids.

Q5: Primary structure of a protein?

Linear sequence of amino acids.

Q6: Fat vs oil at room temperature?

Fat solid/semisolid; oil liquid (saturation vs unsaturation).

Q7: Components of a nucleotide?

Nitrogenous base + pentose + phosphate.

Q8: DNA vs RNA bases?

DNA: A,G,C,T · RNA: A,G,C,U (uracil replaces thymine).

Q9: Watson–Crick base pairs?

A–T and G–C (H-bonds); strands complementary.

Q10: Lock-and-key model?

Substrate fits enzyme active site specifically → ES complex → products.

Q11: Role of insulin?

Polypeptide hormone; regulates glucose metabolism; deficiency → diabetes mellitus.

Q12: Vitamin A deficiency?

Night blindness, dry skin (fat-soluble vitamin).

Section 8: Tips & Exam Hacks

Memory Aids

  • DNA bases: "AT GC" pair · RNA: "U for T"
  • Starch/cellulose: "α store · β structure"
  • Fat/oil: "Solid fat · liquid oil"
  • Essential AA: "Must eat ~10"
  • Vitamins: "ADEK fat · rest water"

Exam Tips

  • Write glycoside and peptide bonds clearly
  • List four protein structure levels with H-bond roles
  • DNA double helix + complementary replication
  • Enzyme = protein + specificity + mild conditions
  • Match vitamins to deficiency symptoms

Section 9: Quick Reference

• Carbs: mono/di/poly · D-glucose · anomers · starch/glycogen/cellulose

• Proteins: α-AA · peptide · 1°–4° · denaturation · fibrous/globular

• Lipids: triglyceride · fat/oil · phospholipid · steroid · ADEK

• Nucleic acids: nucleotide · DNA vs RNA · A–T/G–C · protein code

• Enzymes lock-key · hormones · vitamins + deficiencies

PYQ — Previous Year Questions

Extracted from NIOS Chemistry (313) board exam papers in your PDF. Chapter L29 — Biomolecules only. Use Model Answer for marking points; Explanation for concept clarity.

L29 — Biomolecules

5 question(s) · Sources: 313/MAY/205A, 313/MAY/205B, 313/MAY/205C, 313/TUS/105A

Section A — MCQ / Objective (from papers)

PYQ1. Write True (T) for correct statement and False (F) for incorrect statement : Phospholipids are constituents of the cell membrane. The structure of protein molecule is not changed by changing its temperature. ghr

2 marks · Q27 · 313/MAY/205A

Model Answer

Answer using key concepts from L29 (definitions, equations, and one example where useful). Stay within the suggested word range for a 2-mark NIOS question.

Explanation

Cross-check with L29 notes. Structure: definition/law → working → conclusion. Partial marks for correct equations even if explanation is short.

How to write for NIOS: Use 30–50 words (VSA) or short objective. Open with definition/equation, then reason, end with conclusion. Paper 313/MAY/205A · Q27 · 2 mark(s) · L29.

PYQ2. Write True (T) for correct statement and False (F) for incorrect statement : Phospholipids are constituents of the cell membrane. The structure of protein molecule is not changed by changing its temperature. ghr

2 marks · Q18 · 313/MAY/205B

Model Answer

Answer using key concepts from L29 (definitions, equations, and one example where useful). Stay within the suggested word range for a 2-mark NIOS question.

Explanation

Cross-check with L29 notes. Structure: definition/law → working → conclusion. Partial marks for correct equations even if explanation is short.

How to write for NIOS: Use 30–50 words (VSA) or short objective. Open with definition/equation, then reason, end with conclusion. Paper 313/MAY/205B · Q18 · 2 mark(s) · L29.

PYQ3. Write True (T) for correct statement and False (F) for incorrect statement : Phospholipids are constituents of the cell membrane. The structure of protein molecule is not changed by changing its temperature. ghr

2 marks · Q20 · 313/MAY/205C

Model Answer

Answer using key concepts from L29 (definitions, equations, and one example where useful). Stay within the suggested word range for a 2-mark NIOS question.

Explanation

Cross-check with L29 notes. Structure: definition/law → working → conclusion. Partial marks for correct equations even if explanation is short.

How to write for NIOS: Use 30–50 words (VSA) or short objective. Open with definition/equation, then reason, end with conclusion. Paper 313/MAY/205C · Q20 · 2 mark(s) · L29.

PYQ4. Chemically enzymes are — (A) polysaccharides   (B) polypeptides   (C) polynucleotides   (D) globular proteins amgm¶{

1 mark · Q14 · 313/TUS/105A

Model Answer

Model approach (select the best option):

  • (A) polysaccharides
  • (B) polypeptides
  • (C) polynucleotides
  • (D) globular proteins amgm¶{

Eliminate options that contradict definitions/equations from the chapter notes. NIOS awards full mark for the single correct choice.

Explanation

This MCQ belongs to L29. Recall the core definition or formula from notes, then match it to one option. Paper: 313/TUS/105A · Q14.

Tip: For numerical MCQs, write the formula first, substitute values, then pick the option.

PYQ5. Read the passage given below and answer the following questions (out of four attempt any two) : Hormones are chemical messengers which are secreted by endocrine glands. They are carried through the blood stream to the target tissues. Vitamins are small organic molecules which are taken in diet and these are required in trace amounts for proper-growth. Name a female sex hormone and state its function. Which disease is caused by the deficiency of insulin in humans? Which gland secretes it? Which water-soluble vitamin’s deficiency causes a disease with symptoms of (i) cracked lips, scaly skin and (ii) anaemia, irritability? Name any two vitamins which are fat-soluble.

2 marks · Q27 · 313/TUS/105A

Model Answer

Answer using key concepts from L29 (definitions, equations, and one example where useful). Stay within the suggested word range for a 2-mark NIOS question.

Explanation

Cross-check with L29 notes. Structure: definition/law → working → conclusion. Partial marks for correct equations even if explanation is short.

How to write for NIOS: Use 30–50 words (VSA) or short objective. Open with definition/equation, then reason, end with conclusion. Paper 313/TUS/105A · Q27 · 2 mark(s) · L29.

Problem Solving — L29 Biomolecules

Six problems spanning this chapter’s NIOS syllabus. Every question is built from the notes and formula sheet: solve with equations first, then read the formal textbook-style write-up, the easy explanation, and the topic in depth (formulas, meaning, exam tips). If the question says draw, a labelled pencil sketch is provided. Explanations open by default.

Question 1 of 6Carb

Define monosaccharide and give two examples.

Solution — step by step with formulas

  1. Simple sugars that cannot hydrolyse further; glucose, fructose.

Final answer: Glucose, fructose

Textbook formal language

Carbohydrates are polyhydroxy aldehydes/ketones or derivatives.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

Single sugar units—building blocks of bigger carbs.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — Carbohydrates

Disaccharides hydrolyse to two monosaccharides.

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.
Question 2 of 6Glucose

Is glucose an aldose or ketose? How many carbons?

Solution — step by step with formulas

  1. Aldose; C₆ (aldohexose).

Final answer: Aldohexose

Textbook formal language

Open chain has aldehyde; cyclic hemiacetal forms in solution.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

Six-carbon sugar with aldehyde end in open form.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — Glucose structure idea

α/β anomers at C1 in rings.

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.
Question 3 of 6Protein

What is a peptide bond?

Solution — step by step with formulas

  1. Amide linkage –CO–NH– between amino acids.

Final answer: –CO–NH– between amino acids

Textbook formal language

Proteins are polymers of α-amino acids.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

Amino acids join by condensation—water leaves, peptide forms.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — Proteins

Primary structure is sequence of amino acids.

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.
Question 4 of 6Enzyme

State two features of enzymes as biological catalysts.

Solution — step by step with formulas

  1. Highly specific; lower activation energy; protein nature; optimal pH/T.

Final answer: Specific; protein catalysts

Textbook formal language

Enzymes accelerate reactions under mild conditions.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

Nature’s catalysts—pick one substrate and work fast at body temperature.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — Enzymes

Denatured by heat/extremes of pH.

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.
Question 5 of 6Nucleic

Name the sugar in DNA and the four bases.

Solution — step by step with formulas

  1. Deoxyribose; A,T,G,C.

Final answer: Deoxyribose; A T G C

Textbook formal language

Nucleotides: base + sugar + phosphate.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

DNA uses deoxyribose and thymine; RNA uses ribose and uracil.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — DNA/RNA

Base pairing A–T, G–C in double helix.

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.
Question 6 of 6Vitamin

Classify vitamins as water- or fat-soluble with one example each.

Solution — step by step with formulas

  1. Water: B complex, C; fat: A,D,E,K.

Final answer: Water: B/C; fat: A/D/E/K

Textbook formal language

Deficiency diseases linked to specific vitamins.

Working formulas: (see solution steps). State the definition or law first (NIOS style), use SI units, and box the final numerical answer with unit.

Easy language (same idea, plain words)

Some vitamins wash out in urine; others store in fat.

Read once for the idea, once for the numbers. Write the formula, substitute, then simplify. Check whether you used moles, grams, or litres correctly.

Topic in depth — Vitamins

Vitamin C deficiency → scurvy (classic).

Linked to chapter notes (L29). Remember: (see solution steps). Most exam errors are unit mix-ups (g vs mol, mL vs L) or wrong mole ratios from the equation.

Exam tip

Write (see solution steps) before substituting. Keep three significant figures until the end when data allow.

Common mistakes

  • Confusing mass (g) with amount of substance (mol).
  • Forgetting Avogadro’s number unit mol⁻¹ or STP volume 22.7 L mol⁻¹ (1 bar).
  • Using wrong mole ratio from the balanced equation.
  • Mixing up empirical and molecular formulas.