Biomolecules
Each subtopic includes About section, revision page link, 10 preview questions, and practice CTAs.
Chemical constituents of living cells
SubtopicChemical constituents of living cells under Biomolecules for Grade 11 CBSE.
Preview questions (no answers)
- 1.
Which of the following is NOT a polymeric substance?
A.Nucleic acids
B.Proteins
C.Polysaccharides
D.Lipids
- 2.
Which of the following bonds is characteristic of the primary structure of proteins?
A.Hydrogen bond
B.Disulfide bond
C.Peptide bond
D.Glycosidic bond
- 3.
Inulin is a polymer of which unit?
A.Glucose
B.Fructose
C.Ribose
D.Galactose
- 4.
Which protein is known for its role in transporting glucose into cells?
A.Insulin
B.Collagen
C.GLUT-4
D.Antibody
- 5.
Non-reducing sugars are those that cannot reduce ions. Which of the following is a non-reducing sugar?
A.Glucose
B.Fructose
C.Sucrose
D.Lactose
- 6.
In the double-stranded DNA structure, the two strands are described as:
A.Parallel with 5' to 3' polarity
B.Antiparallel with 5' to 3' and 3' to 5' polarity
C.Randomly coiled without specific polarity
D.Linked together by glycosidic bonds
- 7.
Which of the following is a polymeric secondary metabolite?
A.Abrin
B.Rubber
C.Monoterpenes
D.Carotenoids
- 8.
The chemical and physical properties of amino acids are essentially due to the amino, carboxyl, and the specific R-functional groups. Refer to the classification diagram below where W, X, Y, and Z represent different amino acids distinguished by their R-groups. Which of the following sets correctly identifies these amino acids as described in the standard biochemical classification of living cells?
A.W: Serine, X: Alanine, Y: Glycine, Z: Tyrosine
B.W: Alanine, X: Glycine, Y: Serine, Z: Phenylalanine
C.W: Glycine, X: Alanine, Y: Serine, Z: Tyrosine
D.W: Glycine, X: Serine, Y: Alanine, Z: Tryptophan
- 9.
A biochemist synthesizes a lipid by reacting one molecule of trihydroxy propane with three molecules of a saturated fatty acid that contains exactly 16 carbons (including the carboxyl carbon). Based on the reaction pathway shown below, identify the final product and the total number of water molecules released during this complete esterification process.
A.P: Triarachidonin, n: 3
B.P: Tripalmitin, n: 3
C.P: Tripalmitin, n: 1
D.P: Triarachidonin, n: 1
- 10.
A complete enzyme consisting of an apoenzyme and its co-factor is called a:
A.Pro-enzyme
B.Holoenzyme
C.Iso-enzyme
D.Co-enzyme
Download the worksheet for Biomolecules - Chemical constituents of living cells to practice offline. It includes additional chapter-level practice questions.
Structure and function of Proteins, Carbohydrates, Lipids, Nucleic acids
SubtopicStructure and function of Proteins, Carbohydrates, Lipids, Nucleic acids under Biomolecules for Grade 11 CBSE.
Preview questions (no answers)
- 1.
The helical structure of DNA is maintained by which type of bonds between nitrogenous bases?
A.Covalent bonds
B.Ionic bonds
C.Hydrogen bonds
D.Peptide bonds
- 2.
Which of the following is a nitrogenous base belonging to the pyrimidine group?
A.Adenine
B.Guanine
C.Cytosine
D.Tryptophan
- 3.
What is the ratio of Oxygen to Hydrogen in a typical carbohydrate molecule?
A.1:2
B.2:1
C.1:1
D.3:1
- 4.
Identify the disaccharide composed of two glucose units.
A.Sucrose
B.Lactose
C.Maltose
D.Fructose
- 5.
The following flowchart describes the two structural components of Starch found in plants. Based on the branching pattern and the type of glycosidic linkages shown, identify 'Component B'.
A.Amylose
B.Amylopectin
C.Cellulose
D.Glycogen
- 6.
Co-enzyme Nicotinamide Adenine Dinucleotide (NAD) contains which vitamin?
A.Thiamine
B.Riboflavin
C.Niacin
D.Pyridoxine
- 7.
Which level of protein structure gives a sequence of amino acids (i.e., who is the first, second, etc.)?
A.Primary structure
B.Secondary structure
C.Tertiary structure
D.Quaternary structure
- 8.
Which of the following statements about saturated fatty acids is TRUE?
A.They contain one or more double bonds in the hydrocarbon chain.
B.They are typically liquid at room temperature.
C.They have the maximum number of hydrogen atoms possible per carbon atom.
D.They are primarily found in plant oils like olive oil.
- 9.
Which of the following is a structural protein that is most abundant in the animal world?
A.Hemoglobin
B.Collagen
C.Keratin
D.Albumin
- 10.
In the titration of a simple amino acid like Glycine, what does the term 'Zwitterion' represent?
A.A form with both positive and negative charges, resulting in net zero charge.
B.A form that is completely deprotonated and carries a negative charge.
C.A form that is completely protonated and carries a positive charge.
D.A form that has lost its amino group.
Download the worksheet for Biomolecules - Structure and function of Proteins, Carbohydrates, Lipids, Nucleic acids to practice offline. It includes additional chapter-level practice questions.
Enzymes: Types, properties, enzyme action
SubtopicEnzymes: Types, properties, enzyme action under Biomolecules for Grade 11 CBSE.
Preview questions (no answers)
- 1.
What is the term for the maximum rate of reaction when all enzyme active sites are saturated with substrate?
A.B.Steady state
C.D.Equilibrium constant
- 2.
The name of the international body that classified enzymes into six major classes is:
A.IUPAC
B.IUBMB
C.WHO
D.UNESCO
- 3.
Which of the following is an inorganic cofactor?
A.NAD
B.FAD
C.Zinc ion
D.Biotin
- 4.
What type of bond is commonly formed between an enzyme and its substrate during the transition state?
A.Strong covalent bonds
B.Weak hydrogen or ionic bonds
C.Permanent peptide bonds
D.Metallic bonds
- 5.
Enzymes often require non-protein cofactors to be catalytically active. Based on the components of a functional enzyme shown in the diagram, how do 'Metal Ions' specifically facilitate the catalytic action within the active site?
A.They act as organic molecules, often derived from vitamins, that associate transiently with the apoenzyme during catalysis.
B.They form coordination bonds with the side chains at the active site and simultaneously with the substrate.
C.They constitute the primary proteinaceous part of the enzyme that defines the shape of the active site pocket.
D.They are organic compounds that are permanently and tightly bound to the apoenzyme as prosthetic groups.
- 6.
In the context of enzymatic reactions, what does the term 'activation energy' mean?
A.The energy released when the product is formed.
B.The minimum energy required to reach the transition state from the ground state.
C.The total kinetic energy of the substrate molecules.
D.The energy required to denature the enzyme.
- 7.
Which of the following is a function of the 'Apoenzyme'?
A.It provides the specific three-dimensional structure and active site for binding.
B.It is the non-protein portion that provides chemical groups.
C.It is the inorganic metal ion that stabilizes the transition state.
D.It is the vitamin derivative that carries electrons.
- 8.
Which of the following best explains why the rate of an enzyme-catalyzed reaction decreases as the reaction nears completion?
A.The enzyme is used up in the reaction.
B.The substrate concentration falls below the .
C.The temperature of the system decreases over time.
D.The enzyme changes into its inactive apoenzyme form.
- 9.
The term 'Catalytic Triad' refers to a group of three amino acids specifically arranged in the active site of certain enzymes like Chymotrypsin to facilitate catalysis. This arrangement is an example of:
A.Primary protein structure
B.Secondary protein structure
C.Tertiary or Quaternary structure positioning
D.Linear denaturation
- 10.
Which of the following is an example of a metal-activated enzyme where the metal ion is not a permanent part of the enzyme structure but is required during catalysis?
A.Iron in Cytochrome oxidase
B.Magnesium in Hexokinase
C.Iron in Hemoglobin
D.Cobalt in Vitamin B12
Download the worksheet for Biomolecules - Enzymes: Types, properties, enzyme action to practice offline. It includes additional chapter-level practice questions.