GATE Biotechnology General Biology Syllabus

General Biology syllabus — full chapter and topic list

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

1. 1

   Biochemistry

   7 topics

   • Biomolecules - structure and function
   • Biological membranes
     • Structure
     • Membrane channels and pumps
     • Molecular motors
     • Action potential and transport processes
   • Basic concepts and regulation of metabolism of carbohydrates, lipids, amino acids and nucleic acids
   • Photosynthesis, respiration and electron transport chain
   • Enzymes - Classification, catalytic and regulatory strategies
   • Enzyme kinetics - Michaelis-Menten equation
   • Enzyme inhibition - competitive, non-competitive and uncompetitive inhibition
2. 2

   Microbiology

   9 topics

   • Bacterial classification and diversity
   • Microbial Ecology - microbes in marine, fresh water and terrestrial ecosystems
   • Microbial interactions
   • Viruses - structure and classification
   • Methods in microbiology
   • Microbial growth and nutrition
   • Nitrogen fixation
   • Microbial diseases and host-pathogen interactions
   • Antibiotics and antimicrobial resistance
3. 3

   Immunology

   16 topics

   • Innate and adaptive immunity, humoral and cell mediated immunity
   • Antibody structure and function
   • Molecular basis of antibody diversity
   • T cell and B cell development
   • Antigen-antibody reaction
   • Complement
   • Primary and secondary lymphoid organs
   • Major histocompatibility complex (MHC)
   • Antigen processing and presentation
   • Polyclonal and monoclonal antibody
   • Regulation of immune response
   • Immune tolerance
   • Hypersensitivity
   • Autoimmunity
   • Graft versus host reaction
   • Immunization and vaccines

General Biology flashcards for GATE Biotechnology

21 of 51 cards from the General Biology deck — real questions with worked answers.

1. What are the four major classes of biomolecules in living cells?

   Carbohydrates, lipids, proteins (made of amino acids), and nucleic acids (DNA/RNA).

2. What type of bond links amino acids in a protein, and which reaction forms it?

   A peptide bond (an amide linkage), formed by a dehydration/condensation reaction releasing one water molecule between the $\alpha$-carboxyl of one residue and the $\alpha$-amino of the next.

3. Name the four levels of protein structure and the interaction that mainly stabilizes each.

   Primary (peptide bonds/sequence), secondary ($\alpha$-helix and $\beta$-sheet, stabilized by backbone H-bonds), tertiary (side-chain interactions: H-bonds, ionic, hydrophobic, disulfides), quaternary (subunit assembly via the same non-covalent forces).

4. What is the structural basis of base pairing in DNA, and how many H-bonds form in each pair?

   Complementary Watson–Crick pairing: adenine–thymine with 2 hydrogen bonds and guanine–cytosine with 3 hydrogen bonds; strands run antiparallel ($5'\to3'$ opposite $3'\to5'$).

5. Describe the fluid mosaic model of biological membranes.

   A two-dimensional fluid lipid bilayer (phospholipids, cholesterol, glycolipids) in which integral and peripheral proteins are embedded and can diffuse laterally; lipids and proteins form a dynamic 'mosaic'.

6. What property of phospholipids drives spontaneous bilayer formation in water?

   Their amphipathic nature: hydrophilic phosphate head groups face the aqueous phase while hydrophobic fatty-acid tails sequester inward, minimizing free energy via the hydrophobic effect.

7. Distinguish a membrane channel from a membrane pump.

   A channel forms a gated/passive pore allowing ions to flow down their electrochemical gradient (no energy input); a pump uses energy (e.g., ATP) to move ions/solutes against their gradient (active transport).

8. What does the $\ce{Na+/K+}$-ATPase pump, and in what stoichiometry per ATP?

   It exports $3\,\ce{Na+}$ out and imports $2\,\ce{K+}$ in per ATP hydrolyzed, an electrogenic primary active transporter maintaining the resting membrane gradients.

9. Name three cytoskeletal molecular motors and the tracks they move along.

   Myosin (moves along actin filaments), kinesin (moves toward the plus/+ end of microtubules), and dynein (moves toward the minus/− end of microtubules); all are ATPases.

10. What ionic events generate the rising (depolarization) and falling (repolarization) phases of a neuronal action potential?

    Depolarization: voltage-gated $\ce{Na+}$ channels open and $\ce{Na+}$ rushes in. Repolarization: $\ce{Na+}$ channels inactivate and voltage-gated $\ce{K+}$ channels open, letting $\ce{K+}$ flow out.

11. Compare primary, secondary, and passive transport across membranes.

    Passive (facilitated/simple diffusion): down gradient, no energy. Primary active: uses ATP directly (e.g., $\ce{Na+/K+}$-ATPase). Secondary active: uses an ion gradient (set up by a primary pump) to co-transport another solute (symport/antiport).

12. What is the central principle distinguishing catabolism from anabolism?

    Catabolism breaks down complex molecules to release energy (oxidative, produces ATP/NADH); anabolism builds complex molecules from simpler ones, consuming energy (reductive, uses ATP/NADPH).

13. Which two molecules are the universal currencies of energy and reducing power in metabolism?

    ATP is the energy currency; $\ce{NADH}$/$\ce{FADH2}$ (catabolism) and $\ce{NADPH}$ (anabolism) are the reducing-power carriers.

14. What is the committed and key regulatory step of glycolysis, and which enzyme catalyzes it?

    The phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, catalyzed by phosphofructokinase-1 (PFK-1), allosterically inhibited by ATP/citrate and activated by AMP/F-2,6-BP.

15. What is the rate-limiting enzyme of fatty acid synthesis and what activates it?

    Acetyl-CoA carboxylase (forms malonyl-CoA); activated by citrate and insulin, inhibited by palmitoyl-CoA and glucagon/AMPK phosphorylation.

16. By what general process are amino acids deaminated, and where is the resulting ammonia detoxified?

    By transamination followed by oxidative deamination (glutamate dehydrogenase) releasing $\ce{NH3}$; ammonia is converted to urea via the urea cycle in the liver.

17. Distinguish de novo from salvage pathways of nucleotide synthesis.

    De novo: nucleotides built from scratch using amino acids, $\ce{CO2}$, $\ce{PRPP}$, etc. (energy-expensive). Salvage: recycle free bases/nucleosides from degradation back into nucleotides (energy-saving).

18. Write the overall (net) equation of oxygenic photosynthesis.

    $$\ce{6CO2 + 6H2O ->[light] C6H12O6 + 6O2}$$

19. What are the products of the light-dependent reactions of photosynthesis?

    $\ce{O2}$ (from water splitting), ATP (photophosphorylation), and $\ce{NADPH}$; these supply energy and reducing power to the Calvin cycle.

20. What enzyme fixes $\ce{CO2}$ in the Calvin cycle and what is its first stable product?

    RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) fixes $\ce{CO2}$ onto RuBP, yielding two molecules of 3-phosphoglycerate (3-PGA).

21. Write the overall equation of aerobic cellular respiration.

    $$\ce{C6H12O6 + 6O2 -> 6CO2 + 6H2O}$$ with release of energy captured as ATP.

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