NEET PG Bio Chemistry Syllabus

Bio Chemistry syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Bio Chemistry in NEET PG, not a summary of it.

1. 1

   Molecular Biology

   5 topics

   • Structure and function of nucleic acids: DNA and RNA
   • DNA replication
     • Enzymes involved
     • Replication fork
     • Leading and lagging strands
   • Transcription
     • RNA polymerase
     • mRNA synthesis
     • Transcription factors
     • Regulation
   • Translation
     • Ribosomes
     • tRNA
     • Codons
     • Initiation
     • Elongation
     • Termination
     • Regulation
   • Genetic code
     • Codons
     • Amino acids
     • Start and stop codons
     • Wobble hypothesis
2. 2

   Proteins

   5 topics

   • Amino acids
     • Classification
     • Structure
     • Properties
     • Essential vs. non-essential amino acids
   • Protein structure
     • Primary structure
     • Secondary structure
     • Tertiary structure
     • Quaternary structure
   • Protein folding and stability
     • Chaperones
     • Denaturation
     • Refolding
   • Enzymes
     • Classification
     • Mechanism of enzyme action
     • Kinetics
     • Enzyme regulation
   • Enzyme inhibitors
     • Competitive inhibitors
     • Non-competitive inhibitors
     • Mixed inhibitors
3. 3

   Carbohydrate Metabolism

   5 topics

   • Glycolysis
     • Pathway
     • Enzymes
     • Regulation
     • Energetics
   • Gluconeogenesis
     • Pathway
     • Substrates
     • Enzymes
     • Regulation
   • Pentose Phosphate Pathway
     • Functions
     • Significance
   • Glycogen Metabolism
     • Synthesis
     • Degradation
     • Regulation
   • Citric Acid Cycle (Krebs Cycle)
     • Steps
     • Enzymes
     • Regulation
     • Metabolic Significance
4. 4

   Lipid Metabolism

   4 topics

   • Fatty acid metabolism
     • β-oxidation
     • Synthesis
     • Desaturation
     • Elongation
   • Triacylglycerol metabolism
     • Synthesis
     • Breakdown
     • Regulation
   • Lipoprotein metabolism
     • Classification
     • Structure
     • Functions
     • Role in lipid transport
   • Ketone bodies
     • Synthesis
     • Utilization
     • Regulation
5. 5

   Amino Acid Metabolism

   3 topics

   • Overview of amino acid metabolism
     • Transamination
     • Deamination
     • Urea cycle
   • Metabolism of specific amino acids
     • Glucogenic vs. ketogenic amino acids
   • One-carbon metabolism
     • Methylation reactions
     • Folate metabolism
     • Vitamin B12
6. 6

   Bioenergetics and Oxidative Phosphorylation

   3 topics

   • ATP synthesis
     • Chemiosmotic hypothesis and mitochondrial electron transport chain
   • Regulation of oxidative phosphorylation
   • Mitochondrial disorders and their biochemical basis
7. 7

   Intermediary Metabolism

   2 topics

   • Regulation of metabolic pathways
     • Hormonal regulation
     • Allosteric regulation
     • Covalent modification
   • Integration of metabolism
     • Metabolic interconversions
     • Metabolic flux
     • Energy balance
8. 8

   Hormones and Signal Transduction

   2 topics

   • Hormone classification
     • Endocrine vs. exocrine hormones
     • Peptide hormones
     • Steroid hormones
     • Mechanisms of action
   • Signal transduction pathways
     • Second messengers
     • G-proteins
     • Protein kinases
     • Gene regulation
9. 9

   Nutrition and Vitamins

   2 topics

   • Essential Nutrients
     • Macronutrients (carbohydrates, proteins, fats)
     • Micronutrients (vitamins, minerals)
   • Functions, Sources, and Deficiencies of Vitamins
     • Fat-soluble vitamins (A, D, E, K)
     • Water-soluble vitamins (B-complex, C)
10. 10

    Biochemical Techniques

    1 topic

    • Principles and applications of biochemical techniques
      • Spectrophotometry
      • Chromatography
      • Electrophoresis
      • PCR
      • DNA sequencing
      • Recombinant DNA technology

Bio Chemistry flashcards for NEET PG

24 of 60 cards from the Bio Chemistry deck — real questions with worked answers.

1. What are the structural differences between DNA and RNA in terms of sugar, bases, and strands?

   DNA: deoxyribose sugar, bases A-T-G-C, usually double-stranded. RNA: ribose sugar, bases A-U-G-C (uracil replaces thymine), usually single-stranded.

2. In the DNA double helix, which base pairs together and by how many hydrogen bonds?

   Adenine pairs with Thymine (2 hydrogen bonds); Guanine pairs with Cytosine (3 hydrogen bonds).

3. What does Chargaff's rule state about DNA base composition?

   In double-stranded DNA, A = T and G = C; thus purines (A+G) equal pyrimidines (T+C).

4. Why is DNA replication described as semiconservative?

   Each daughter DNA molecule contains one parental (old) strand and one newly synthesized strand. Proven by the Meselson-Stahl experiment.

5. What is the function of DNA polymerase III versus DNA polymerase I in prokaryotic replication?

   Pol III is the main replicating enzyme synthesizing the leading and lagging strands; Pol I removes RNA primers (5'->3' exonuclease) and fills gaps.

6. Why is the lagging strand synthesized in Okazaki fragments?

   DNA polymerase only synthesizes 5'->3'. On the lagging strand, the template runs in the opposite direction to fork movement, so synthesis occurs discontinuously as short Okazaki fragments later joined by DNA ligase.

7. Which enzyme synthesizes mRNA during transcription and in which direction?

   RNA polymerase synthesizes mRNA in the 5'->3' direction, reading the template (antisense) strand 3'->5'. No primer is required.

8. What are the three main post-transcriptional modifications of eukaryotic mRNA?

   1) 5' 7-methylguanosine cap, 2) 3' poly-A tail, 3) splicing to remove introns and join exons.

9. During translation, what are the three sites of the ribosome and their roles?

   A site (aminoacyl) accepts incoming aminoacyl-tRNA; P site (peptidyl) holds the growing peptide chain; E site (exit) releases deacylated tRNA.

10. What is the start codon and which amino acid does it code for in eukaryotes vs prokaryotes?

    AUG is the start codon; codes for methionine in eukaryotes and formylmethionine (fMet) in prokaryotes.

11. Name the three stop (nonsense) codons.

    UAA, UAG, and UGA.

12. What does it mean that the genetic code is degenerate (redundant)?

    Multiple codons can specify the same amino acid (e.g., 6 codons for leucine), but each codon specifies only one amino acid (unambiguous).

13. What is the wobble hypothesis in relation to the genetic code?

    The third base (3') of a codon can form non-standard pairing with the tRNA anticodon, allowing a single tRNA to recognize multiple codons for the same amino acid.

14. Which amino acids are essential (must be obtained from diet)?

    Phenylalanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine (semi/conditionally), Leucine, Lysine (mnemonic: PVT TIM HALL).

15. At physiological pH, what is the charge state of an amino acid (zwitterion)?

    It exists as a zwitterion: protonated amino group (-NH3+) and deprotonated carboxyl group (-COO-), giving a net neutral charge.

16. Which amino acid is achiral and which contains a secondary amino group (imino acid)?

    Glycine is achiral (no chiral center); proline is an imino acid with a secondary amino group in a ring.

17. What are the four levels of protein structure?

    Primary (amino acid sequence), Secondary (alpha-helix, beta-sheet via H-bonds), Tertiary (3D folding of a polypeptide), Quaternary (assembly of multiple subunits).

18. What bonds stabilize the secondary structure of proteins?

    Hydrogen bonds between backbone carbonyl oxygen and amide hydrogen (forming alpha-helices and beta-pleated sheets).

19. What role do chaperones play in protein folding?

    Molecular chaperones (e.g., HSP70, chaperonins like GroEL/GroES) assist proper folding and prevent aggregation of misfolded proteins, without being part of the final structure.

20. What is the relationship between protein misfolding and disease (example)?

    Misfolded proteins can aggregate causing disease, e.g., prion diseases (alpha-helix converts to beta-sheet), Alzheimer's (amyloid-beta), and Parkinson's (alpha-synuclein).

21. How do enzymes increase reaction rate thermodynamically?

    They lower the activation energy (Ea) of a reaction without changing the equilibrium or the free energy (delta G) of the overall reaction.

22. State the Michaelis-Menten equation and what Km represents.

    v = (Vmax * [S]) / (Km + [S]). Km is the substrate concentration at half-maximal velocity; it inversely reflects enzyme affinity for substrate (low Km = high affinity).

23. How does competitive inhibition affect Km and Vmax?

    Competitive inhibition increases (apparent) Km but Vmax is unchanged, because the inhibitor competes at the active site and can be overcome by excess substrate.

24. How does non-competitive inhibition affect Km and Vmax?

    Non-competitive inhibition decreases Vmax but Km is unchanged, because the inhibitor binds an allosteric site and cannot be overcome by adding more substrate.

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