BDS Admission Test Biology Syllabus

Biology syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Biology in BDS Admission Test, not a summary of it.

1. 1

   Biomolecules

   5 topics

   • Carbohydrates
   • Proteins
   • Lipids
   • Nucleic acids (DNA and RNA)
   • Water and its biological importance
2. 2

   Cell Structure and Function

   4 topics

   • Prokaryotic and eukaryotic cells
   • Cell membrane and transport
   • Cell organelles
   • Nucleus and chromosomes
3. 3

   Enzymes

   4 topics

   • Enzyme structure and characteristics
   • Mechanism of enzyme action
   • Factors affecting enzyme activity
   • Enzyme inhibition
4. 4

   Cell Division

   4 topics

   • Cell cycle
   • Mitosis
   • Meiosis
   • Significance and abnormalities of cell division
5. 5

   Bioenergetics

   3 topics

   • Photosynthesis
   • Respiration
   • ATP as energy currency
6. 6

   Coordination and Control

   3 topics

   • Nervous system
   • Endocrine system and hormones
   • Receptors and effectors
7. 7

   Reproduction

   4 topics

   • Sexual and asexual reproduction
   • Human reproductive system
   • Gametogenesis
   • Reproductive health
8. 8

   Genetics

   4 topics

   • Mendelian inheritance
   • Gene linkage and crossing over
   • Sex determination and sex-linked inheritance
   • Genetic disorders and mutations
9. 9

   Biotechnology

   3 topics

   • Recombinant DNA technology
   • Genetic engineering
   • Applications in medicine and industry
10. 10

    Evolution

    3 topics

    • Lamarckism and Darwinism
    • Evidence of evolution
    • Natural selection

Biology flashcards for BDS Admission Test

22 of 60 cards from the Biology deck — real questions with worked answers.

1. What is the general molecular formula of carbohydrates?

   Cn(H2O)n — carbon, hydrogen and oxygen, with hydrogen to oxygen in a 2:1 ratio (as in water).

2. Define monosaccharides and give three examples.

   Monosaccharides are the simplest single-unit sugars that cannot be hydrolyzed further. Examples: glucose, fructose and galactose (all hexoses, C6H12O6).

3. Name the bond that joins two monosaccharides in a disaccharide and the reaction that forms it.

   A glycosidic bond, formed by a condensation (dehydration) reaction that removes a water molecule.

4. Give the three common disaccharides and the monosaccharides that make up each.

   Maltose = glucose + glucose; Sucrose = glucose + fructose; Lactose = glucose + galactose.

5. Name three polysaccharides and the function of each.

   Starch (energy storage in plants), glycogen (energy storage in animals), and cellulose (structural component of plant cell walls).

6. What is the difference between starch and cellulose in their glycosidic linkages?

   Starch is built from alpha-glucose (alpha-1,4 and alpha-1,6 bonds, digestible), while cellulose is built from beta-glucose (beta-1,4 bonds, indigestible by humans).

7. What are the building blocks (monomers) of proteins?

   Amino acids — there are 20 standard amino acids.

8. Draw/describe the general structure of an amino acid.

   A central (alpha) carbon bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom, and a variable R (side) group.

9. What bond links amino acids together in a protein, and how is it formed?

   A peptide bond, formed by a condensation reaction between the carboxyl group of one amino acid and the amino group of another, releasing water.

10. Describe the primary structure of a protein.

    The linear sequence of amino acids in a polypeptide chain, held together by peptide bonds.

11. What are the two main types of secondary protein structure and the bonds that stabilize them?

    The alpha-helix and beta-pleated sheet, both stabilized by hydrogen bonds between backbone atoms.

12. What is the tertiary structure of a protein?

    The overall three-dimensional folded shape of a single polypeptide, stabilized by R-group interactions: hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.

13. What is quaternary structure? Give an example.

    The arrangement of two or more polypeptide chains (subunits) into a functional protein. Example: hemoglobin (4 subunits).

14. What is denaturation of a protein, and name two factors that cause it.

    Loss of a protein's three-dimensional structure (and thus its function) without breaking peptide bonds. Caused by heat, extreme pH, heavy metals, or organic solvents.

15. What are the elements that make up lipids?

    Carbon, hydrogen, and oxygen — but with a much lower proportion of oxygen than carbohydrates.

16. What are the building blocks of a triglyceride (fat)?

    One molecule of glycerol and three fatty acids, joined by ester bonds (condensation reactions).

17. What bond joins glycerol to fatty acids in a lipid?

    An ester bond, formed by condensation (esterification).

18. Distinguish between saturated and unsaturated fatty acids.

    Saturated fatty acids have no C=C double bonds (single bonds only, solid at room temp); unsaturated fatty acids have one or more C=C double bonds (liquid at room temp, e.g., oils).

19. Describe the structure of a phospholipid.

    A glycerol backbone with two fatty acid tails (hydrophobic) and a phosphate group (hydrophilic head), making it amphipathic — the basis of cell membranes.

20. Name four important biological functions of lipids.

    Long-term energy storage, thermal insulation, protection of organs, and forming cell membranes; steroids also act as hormones.

21. What are the three components of a single nucleotide?

    A pentose sugar, a phosphate group, and a nitrogenous base.

22. Name the nitrogenous bases found in DNA.

    Adenine (A), Guanine (G), Cytosine (C), and Thymine (T).

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