INI CET 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 INI CET, 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 INI CET

24 of 50 cards from the Bio Chemistry deck — real questions with worked answers.

1. What are the structural differences between DNA and RNA?

   DNA has deoxyribose sugar, is usually double-stranded, and uses thymine; RNA has ribose sugar (2'-OH), is usually single-stranded, and uses uracil instead of thymine.

2. Which base pairs form in DNA and how many hydrogen bonds hold each?

   Adenine pairs with Thymine via 2 hydrogen bonds; Guanine pairs with Cytosine via 3 hydrogen bonds. GC-rich DNA is therefore more stable (higher melting temperature).

3. In which direction is a new DNA strand synthesized, and why is one strand discontinuous?

   Synthesis is always 5' to 3'. Because the two parental strands are antiparallel, the leading strand is made continuously while the lagging strand is made discontinuously as Okazaki fragments.

4. What is the function of DNA helicase, primase, and DNA ligase in replication?

   Helicase unwinds the double helix; primase synthesizes RNA primers to start synthesis; DNA ligase seals nicks between Okazaki fragments by forming phosphodiester bonds.

5. What is the role of RNA polymerase in transcription, and does it require a primer?

   RNA polymerase synthesizes RNA from a DNA template in the 5'-to-3' direction; unlike DNA polymerase, it does NOT require a primer to initiate.

6. Name the three main types of RNA and their roles in protein synthesis.

   mRNA carries the genetic message (codons); tRNA brings amino acids and reads codons via its anticodon; rRNA forms the catalytic core of the ribosome.

7. What are the three stages of translation?

   Initiation (ribosome assembles at the start codon), elongation (peptide bonds form as the ribosome moves along mRNA), and termination (release at a stop codon).

8. Which ribosomal activity catalyzes peptide bond formation, and what is unusual about it?

   Peptidyl transferase activity catalyzes peptide bond formation; it is a ribozyme, meaning the catalyst is rRNA (RNA), not protein.

9. What are the start and stop codons of the standard genetic code?

   The start codon is AUG (codes for methionine); the stop codons are UAA, UAG, and UGA.

10. What are the key features of the genetic code (degeneracy, universality, non-overlapping)?

    It is degenerate (multiple codons per amino acid), nearly universal, non-overlapping, comma-less, and read as triplet codons in a fixed reading frame.

11. How are amino acids classified by R-group polarity?

    Nonpolar/hydrophobic, polar uncharged, acidic (negatively charged: Asp, Glu), and basic (positively charged: Lys, Arg, His).

12. Which amino acids are essential in humans?

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

13. Define the four levels of protein structure.

    Primary: amino acid sequence; Secondary: local folding (alpha-helix, beta-sheet) via H-bonds; Tertiary: overall 3D fold of one chain; Quaternary: assembly of multiple subunits.

14. What bonds stabilize the tertiary structure of a protein?

    Hydrophobic interactions, hydrogen bonds, ionic (salt) bridges, and covalent disulfide bonds between cysteine residues.

15. What is the role of molecular chaperones in protein folding?

    Chaperones (e.g., heat-shock proteins like Hsp70) assist correct folding and prevent aggregation of partially folded polypeptides, without being part of the final structure.

16. What is an enzyme and how does it speed up reactions?

    An enzyme is a biological catalyst (usually protein) that lowers the activation energy of a reaction by stabilizing the transition state, without being consumed.

17. Define Km and Vmax in Michaelis-Menten kinetics.

    Vmax is the maximum reaction velocity at saturating substrate; Km is the substrate concentration at half Vmax and reflects enzyme-substrate affinity (low Km = high affinity).

18. How do competitive, non-competitive, and uncompetitive inhibitors affect Km and Vmax?

    Competitive: increases apparent Km, Vmax unchanged. Non-competitive: Km unchanged, Vmax decreased. Uncompetitive: both Km and Vmax decreased.

19. What is the net ATP and NADH yield of glycolysis per glucose?

    Net gain of 2 ATP (4 produced minus 2 used) and 2 NADH, plus 2 pyruvate molecules.

20. Which enzyme is the key irreversible regulatory (rate-limiting) step of glycolysis?

    Phosphofructokinase-1 (PFK-1); it is activated by AMP and fructose-2,6-bisphosphate and inhibited by ATP and citrate.

21. What is the purpose of gluconeogenesis, and where does it primarily occur?

    It synthesizes glucose from non-carbohydrate precursors (lactate, glycerol, glucogenic amino acids) to maintain blood glucose; mainly in the liver (and kidney).

22. What are the two main products and purposes of the Pentose Phosphate Pathway?

    NADPH (for reductive biosynthesis and antioxidant defense) and ribose-5-phosphate (for nucleotide synthesis); the rate-limiting enzyme is glucose-6-phosphate dehydrogenase.

23. Which enzymes carry out glycogen synthesis and breakdown, and what regulates them?

    Glycogen synthase builds glycogen; glycogen phosphorylase breaks it down. Glucagon/epinephrine (via cAMP-PKA) activate phosphorylase and inhibit synthase; insulin reverses this.

24. What enzyme deficiency causes von Gierke disease (Type I glycogen storage disease)?

    Glucose-6-phosphatase deficiency, causing severe fasting hypoglycemia, hepatomegaly, and lactic acidosis.

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