Course Syllabus
Click to Expand: Biochemistry Syllabus (BOT-H-CC11-5-Th)
Semester V (Core)
BOT-H-CC11-5-Th – Biochemistry (Theory) – 75 Marks / 3 Credits
1. Biochemical Foundations
- 1.1 Covalent and non-covalent bonds; hydrogen bond; Van der Waals forces.
- 1.2 Structure andproperties of water.
- 1.3 pH and buffer (inorganic and organic).
- 1.4 Handerson-Hasselbalchequation.
- 1.5 Isoelectric point. (6 lectures)
2. Molecules of Life
- 2.1 Nucleic Acids – structure of nucleosides and nucleotides ; oligo and polynucleotides , A, B & Z form of DNA, RNA- different forms; nucleotide derivatives (ATP, NADP),Hoogstein base pairing of nucleic acids, Concept of sugar puckering and base stacking; torsion angle and supercoiling of nucleic acid.
- 2.2 Proteins – structure and classification of amino acids; primary, secondary, tertiary and quaternary structure of proteins;Protein folding: Leventhal paradox; principles of protein purification.
- 2.3 Carbohydrates - Structure of Carbohydrate: stereochemistry – Fischer projection, Haworth perspective, boat and chair conformation, enantiomers and epimers; inverted sugar, derivative sugar.
- 2.4 Lipids - structure of simple lipid and compound lipid (phospholipids and glycolipids), major classes of storage and structural lipids; fatty acids- saturated and unsaturated; Essential fatty acids; Triacylglycerols structure, functions and properties. (20 lectures)
3. Enzymology
- 3.1 Enzymes – classification and nomenclature (IUBMB); Co-factors and co-enzymes; isozymes.
- 3.2 Enzyme activity and specificity, active site, activation energy, Reaction rate, Mechanism of enzyme action; enzyme inhibition.
- 3.3 Enzyme kinetics (Michaelis - Menten equation and Lineweaver Burk plot), simple problems on enzyme kinetics. (10 lectures)
4. Cell Membrane
- 4.1 Membrane chemistry.
- 4.2 Membrane transport (uniport, symport, antiport), mechanism of ion uptake. (5 lectures)
5. Signal Transduction
- Signal transduction: Basic concept of signal transduction, receptor-ligand interactions, calcium signalling, Cyclic AMP, G protein, MAP-kinase cascade. (5 lectures)
6. Bioenergetics
- Laws of thermodynamics, concept of free energy, endergonic and exergonic reactions, coupled reactions, redox reactions. ATP: structure, its role as energy currency molecule. Energy rich bonds - phosphoryl group transfer. (5 lectures)
Previous Year Questions
2025
BOTANY — HONOURS
Paper : DSCC-11
(Biochemistry)
Full Marks : 75
1. Answer any six questions of the following:
2 × 6
(a) What is 'Isoelectric point'?
(b) Name an acidic and an aromatic amino acid.
(c) What is miRNA?
(d) What property of protein is used in protein purification by 'Ion exchange chromatography'?
(e) Km values of two enzymes are provided below. Which of these two enzymes have higher affinity for its substrate and why?
(i) Carbonic anhydrase = 2.6 × 10⁻² M
(ii) Triose isomerase = 4.7 × 10⁻⁴ M
(i) Carbonic anhydrase = 2.6 × 10⁻² M
(ii) Triose isomerase = 4.7 × 10⁻⁴ M
(f) Write down the structure of the fatty acid – 20:4 (Δ5, 8, 11, 14).
(g) What is the utility of 'Henderson - Hasselbalch equation'?
(h) What are enantiomers? Give an example.
(i) Write down the significance of 'redox potential'.
2. Answer any three questions:
5 × 3
(a) Write a short note on essential fatty acids. (5)
(b) Write down the classes of enzymes as per IUBMB. Cite one example from each class. (5)
(c) 'All monosaccharides are reducing sugars but not all disaccharides.' — Justify. Mention the types of polysaccharides found in plants. (3+2)
(d) Give concise idea of rancidity and saponification. (3+2)
(e) Describe the properties and functions of triacylglycerol. (2½+2½)
3. Answer any four questions:
12 × 4
(a) Define free energy, entropy and enthalpy. Write down the relation between them. What is coupled reaction? Cite an example. What is redox potential? Write down the structure and role of ATP as an energy currency. (3+1+1+1+1+2+3)
(b) Briefly write the general sequence of a cellular signal development. Write in short about second messenger. Explain signal transduction mechanism involving MAP kinase. (3+3+6)
(c) Describe β pleated sheets. Explain salt precipitation method of protein purification. How are peptide bond and polypeptide chain formed among the constituent amino acids of proteins? (5+4+3)
(d) What are the different classes of structural lipids and storage lipids? Write the generic formula of triglyceride. Define PUFA with example. Why are membrane lipids called amphipathic? (5+1+3+3)
(e) Give an overview of cell membrane transport mechanism with reference to symport, antiport and uniport. (4+4+4)
(f) Draw and describe the different forms of DNA. Discuss the differences between mRNA and tRNA. (8+4)
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