Question 10.1
What are monosaccharides?
They cannot be broken into smaller carbohydrates by hydrolysis.
Answer
Examples: glucose, fructose.
CLASS 12 · CHEMISTRY · CHAPTER 10
Simple answers to all 25 current end-of-chapter questions.
25 worked answers · short steps first, explanations when you need them
Textbook pages 302–303
Question 10.1
They cannot be broken into smaller carbohydrates by hydrolysis.
Examples: glucose, fructose.
Question 10.2
They reduce Tollens' or Fehling's reagent.
Glucose and maltose are examples.
Question 10.3
Energy storage (starch) and structural support (cellulose).
Energy storage and cell-wall structure.
Question 10.4
Separate the single-unit sugars from the paired sugars.
Mono: ribose, 2-deoxyribose, galactose, fructose. Di: maltose, lactose.
Question 10.5
Two sugars join and release water.
The connecting C–O–C bond is the glycosidic linkage.
Question 10.6
Both store glucose; glycogen is the animal form and is more branched.
Glycogen is the more highly branched storage carbohydrate of animals.
Question 10.7
Break each disaccharide into its two monosaccharides.
Sucrose → glucose + fructose; lactose → glucose + galactose.
Question 10.8
The glucose form and glycosidic linkage differ.
Starch: α-glucose. Cellulose: β-glucose, β(1→4) links.
Question 10.9
HI reduces; bromine water oxidises the aldehyde; HNO₃ oxidises both ends.
n-Hexane; gluconic acid; saccharic acid.
Question 10.10
The α and β forms and mutarotation are key evidence for ring formation.
Glucose mainly has a cyclic hemiacetal structure.
Question 10.11
Essential amino acids must come from food; the body can make non-essential ones.
Examples: essential—valine, lysine; non-essential—glycine, alanine.
Question 10.12
Define the bond, sequence and shape change.
Peptide bond; amino-acid sequence; loss of natural shape/activity.
Question 10.13
These are regular folds stabilised by hydrogen bonds.
α-Helix and β-pleated sheet.
Question 10.14
Backbone peptide groups form hydrogen bonds.
Hydrogen bonds.
Question 10.15
Compare shape, solubility and role.
Globular: compact, often soluble. Fibrous: long, usually insoluble and structural.
Question 10.16
–COOH donates H⁺; –NH₂ accepts H⁺.
Amino acids are amphoteric.
Question 10.17
They catalyse reactions in living systems.
Biological catalysts.
Question 10.18
The folded shape is disrupted; function is usually lost.
Secondary/tertiary structure changes; primary structure usually remains.
Question 10.19
Group vitamins by solubility.
Fat-soluble A, D, E, K; water-soluble B, C. Clotting: K.
Question 10.20
A: vision and tissue health. C: connective tissue and healing.
Sources: A—carrot, milk, eggs; C—citrus, amla, guava.
Question 10.21
DNA and RNA are nucleotide polymers.
They carry genetic information and support protein synthesis.
Question 10.22
A nucleotide has phosphate; a nucleoside does not.
Base + sugar; base + sugar + phosphate.
Question 10.23
A pairs with T; G pairs with C.
The strands have matching complementary sequences.
Question 10.24
Compare sugar, base, strands and role.
DNA stores hereditary information; RNA mainly helps protein synthesis.
Question 10.25
Each type supports a different part of protein synthesis.
Messenger, transfer and ribosomal RNA.