Biochemistry Important Questions are most helpful for the B.Pharm 2nd semester examination. You can also download the suggestions PDF.
Chemistry of Carbohydrates
1. Explain the term carbohydrate.
2. Give a detailed classification of carbohydrates.
3. Write short notes on the following:
(a) Non-reducing sugar (sucrose)
(b) Lactose
(c) Glycosaminoglycans
(d) Structure of starch and glycogen.
4. Explain the term isomerism. Give the salient features of stereoisomerism in carbohydrates.
5. Define mutarotation.
6. Why is sucrose known as invert sugar?
7. Define epimer. Give examples of the same.
8. What is the difference between a disaccharide and a polysaccharide?
9. Which test will you perform to detect the presence of reducing sugar? Explain the principle of the same test.
10. Give an account of the biological importance of glucose.
11. Describe the structure and function of mucopolysaccharides.
12. Discuss the structure and function of homopolysaccharides.
13. Outline the salient features of the importance of glycosaminoglycans.
14. Define a glycoside. Explain the glycoside formation with a neat labelled diagram.
15. What is the biological significance of glycoproteins?
16. Explain the action of phenylhydrazine on the glucose molecule.
Chemistry of Amino Acids and Proteins
1. Describe the classification of amino acids along with their structures.
2. Give an account of the classification of proteins with suitable examples.
3. Give a classification of amino acids on the basis of nutrition.
4. Write a detailed note on the various levels of organization of protein structures with suitable examples.
5. Explain the classification of proteins with suitable examples.
6. Write notes on:
(a) Zwitter ion.
(b) Isoelectric pH of amino acids.
(c) α-helix.
(d) Tertiary structure of protein.
7. What is the importance of primary structure of protein?
8. Explain in detail the structure of the β-pleated sheet.
9. What is meant by the secondary structure of a protein? Add a note on the α-helical structure.
10. Why do we call some amino acids as glucogenic and some as ketogenic? Enlist the members of the glucogenic and ketogenic amino acids.
Chemistry of Lipids
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Bioenergetics
1. Explain the concept of free energy.
2. Determine free energy from the equilibrium constant.
3. What are energy rich compounds. Give their importance.
4. Explain with structures:
(a) Phosphocreatine
(b) Phosphoenolpyruvate
(c) Thioesters
(d) 3′,5′-Cyclic AMP (cAMP)
5. Describe the major biochemical function of cyclic AMP.
Carbohydrates Metabolism
1. Describe the pathway of aerobic glycolysis.
2. Why is pyruvate kinase considered a key glycolytic enzyme?
3. How is the glycolysis pathway regulated?
4. What is the significance of the TCA cycle?
5. Explain functions and energetics of the TCA Cycle.
6. What is the significance of the Pentose Phosphate Pathway?
7. Write a note on glycogenesis and glycogenolysis.
8. Define and describe in detail, gluconeogenesis.
9. Describe the importance of the transaldolase reaction of the pentose phosphate pathway.
10. What are the cellular sites of (i) Glycolysis, (ii) TCA cycle, (iii) Pentose phosphate pathway, (iv) Gluconeogenesis, (v) Glycogenesis, (vi) Glycogenolysis?
Diabetes Mellitus and Insulin
1. Define diabetes. Explain its various types.
2. Write a note on juvenile onset diabetes.
3. What is the rationale behind screening of HbA1c in diabetic patients?
4. What is meant by OGTT? What is the prerequisite condition for the same?
5. Explain in detail – metabolic changes occurring in diabetes.
6. Give a brief account of the complications in diabetes. Write the biochemical bases for the same.
7. Explain the different measures necessary to treat the different types of diabetes.
Biological Oxidation
1. Explain the structure of mitochondria. Draw and label the necessary diagram.
2. Write a note on the Electron transport chain.
3. Give only the flow sheet of the electron transport chain, with special mention of various inhibitors and their sites.
4. Define oxidative phosphorylation. What is the cellular site of oxidative phosphorylation?
5. Describe in detail the chemiosmotic hypothesis of oxidative phosphorylation.
6. Give an account of the energetics of oxidative phosphorylation.
7. What is meant by electron carriers of the respiratory chain? What is the mode and sequence of electron transport across the respiratory chain?
8. Write short notes on:
(a) Chemical coupling hypothesis.
(b) Conformational coupling hypothesis.
(c) Nicotinamide as an electron carrier.
(d) Iron sulfur proteins.
(e) ATP synthesis.
9. Explain the role of flavoproteins in the Electron transport chain.
10. What is meant by cytochromes? How do they participate in the respiratory chain?
11. Explain in detail working of respiratory chain in mitochondria with a special mention of various sites of ATP synthesis.
12. Define oxidative phosphorylation. Write a note on P:O ratio.
13. Explain the role played by co-enzyme Q in the electron transport chain.
14. Describe the respiratory control of oxidative phosphorylation.
15. Explain in detail: Inhibition of oxidative phosphorylation.
16. Give an account of enzymes participating in oxidative phosphorylation.
17. Explain in detail “High Energy Compounds”.
18. Discuss ATP-ADP cycle in the biological system.
19. Give a detailed account of inborn errors of oxidative phosphorylation.
Metabolism of Lipids
1. Explain in detail the pathway of fatty acid biosynthesis.
2. Highlight the salient features of the β-oxidation of fatty acid.
3. Give the energetics of the β-oxidation of C16 fatty acid.
4. How many numbers of ATPs will be produced, if the C20 fatty acid is completely oxidised to CO2 and H2O?
5. Explain in detail the pathway for cholesterol biosynthesis.
6. Discuss in detail the metabolism of phospholipids, lecithin and cephalin.
7. What is meant by ketone bodies? What is their biochemical significance?
8. Describe in short synthesis of ketone bodies.
9. Describe the pathway for the production of steroid hormones from cholesterol.
10. Write short notes on: (a) Obesity (b) Lipotropic factors. (c) Atherosclerosis
Metabolism of Amino Acids and Proteins
1. Define inborn errors of metabolism. Add a detailed note on the inborn errors of amino acid metabolism.
2. Describe in detail the pathway of catabolism of amino acids tyrosine and phenylalanine.
3. Write a brief account ofthe catabolism of sulphur containing amino acids.
4. Explain the fate of the carbon skeleton of amino acids.
5. Write notes on the catabolism of the following amino acids:
(a) Histidine, (b) Proline, (c) Arginine, (d) Valine, (e) Leucine, (f) Isoleucine
6. Explain in detail the pathway for the synthesis of thyroid hormone.
7. Write a note on the pathway of synthesis of catecholamines.
8. Explain the importance of glycine in the synthesis of specialised products in biochemistry.
9. Explain the pathway for the synthesis of urea.
10. Define transamination. Add a note on the significance and mechanism of the same.
11. What is meant by deamination? Write a note on the same.
12. Give an account of the significance of the one-carbon metabolism in biochemistry.
13. Write notes on: (a) Cystinuria (b) Catabolism of serine (c) Nitrogen balance (d) Amino acid biosynthesis
Chemistry and Metabolism of Nucleotides
1. Explain the sources of different atoms in purine nucleotides.
2. Write a note on the de novo synthesis of purine nucleotides.
3. What is meant by the salvage pathway? Add a note on the salvage pathway for purine nucleotide biosynthesis.
4. Explain the metabolic pathway for the biosynthesis of the pyrimidine nucleotides.
5. Discuss the de novo pathway for purine nucleotide biosynthesis.
6. Write short notes on:
(a) Regulation of pyrimidine nucleotide biosynthesis.
(b) Regulation of purine nucleotide biosynthesis.
(c) Metabolic disorders associated with catabolism of purine nucleotides.
(d) Inhibitors of purine synthesis.
(e) Role of carbamoyl phosphate synthetase II.
7. Explain in detail the biosynthesis of inosine monophosphate.
8. Describe in detail the role of PRPP in purine and pyrimidine biosynthesis.
9. Explain with flow chart catabolism of purine nucleotides.
10. Describe in detail the terms – gout and hyperuricemia.
DNA Replication and Recombinant DNA Technology
1. Explain the replication of DNA with a neat, labeled diagram.
2. Give an account of the roles of various proteins in the replication of DNA.
3. Describe the salient features of DNA replication in eukaryotes.
4. Write a note on the polymerase chain reaction.
5. Describe the terms replication fork and Okazaki pieces.
6. Write notes on:
(a) DNA polymerase I
(b) Meselson and Stahl experiment.
(c) Role of helicases in replication.
(d) Replication fork.
(e) Recombinant DNA technology.
(f) Restriction endonucleases.
7. Define mutation. Explain various types of the same. Add a note on the DNA repair.
8. Give the significance of hybridization techniques.
9. Explain in detail the significance of rDNA technology.
RNA, Transcription, and Transition
Transcription
1. Define transcription. Add a note on transcription in prokaryotes and eukaryotes.
2. Enlist the proteins participating in transcription. Describe the role of each protein in short.
3. Write short notes on:
(a) Role of mRNA in transcription.
(b) RNA chain termination.
(c) Inhibitors of transcription.
4. Give a schematic representation of a transcription bubble.
Transition
1. Define the term genetic code and discuss its characteristic features.
2. Explain in detail protein biosynthesis.
3. What is meant by inhibitor? Add a note on the inhibitors of translation.
4. Write short notes on:
(a) Ribosomes
(b) Codon-anticodon interactions.
(c) Inhibition of translation.
5. Explain the role of tRNA in translation. Give a schematic representation of tRNA.
6. What is meant by polyribosomes? Add a note on the role of polyribosomes in protein synthesis.
Enzymes and Co-enzymes
1. Explain in detail the classification of enzymes according to IUB and nomenclature.
2. Give an account of various models describing the mechanism of enzyme action.
3. Write a note on the effect of substrate concentration on the activity of enzymes.
4. Enlist the different factors affecting the activity of the enzyme. Add a note on the role of the individual factor.
5. Define inhibitor and inhibition. Describe in detail reversible inhibition.
6. Explain the irreversible inhibition with proper examples.
7. Give the salient features of allosteric inhibition.
8. Define isoenzymes. State the characteristics and significance of isoenzymes in biochemistry.
9. Explain in detail the clinical significance of various isoenzymes.
10. Describe the importance of feedback regulation in biochemistry.
11. Define coenzymes. How do they differ from cofactors? Discuss the role of vitamins and non-vitamin co-enzymes in biochemical reactions.
12. Prepare a note on the mechanism of enzyme action.
13. Write short notes on:
(a) Ribozymes
(b) Catalytic mechanisms
(c) Pharmaceutical importance of enzymes.
(d) Restriction enzymes.