In this post, we are including 2010-2021 Previous Year (Regular) and 2016-2021(Supplementary) Papers of Biochemistry. This is based on WBUHS.
PAPER 1
• Enzyme and Membrane Transporters
• Chemistry and Metabolism of Carbohydrates
• Chemistry and Metabolism of Lipids
• Chemistry and Metabolism of Proteins
• Nucleotide Metabolism.
• AETCOM
PAPER 2
• Molecular Biology
• Nutrition
• Extracellular Matrix
• Biological Oxidation
• Oncogenesis and Immunity.
CELL & MEMBRANE TRANSPORT
GROUP-A
1. Discuss how the fluidity of plasma membrane largely depends on its lipid composition. Describe how the macro molecules are transported across the plasma membrane. Explain the role of ion channel, lipid rafts and caveolae.[6+4+2] [2017-S]
2. Discuss how macromolecules are transported across plasma membrane with schematic diagram wherever applicable[8+4][2018-S]
GROUP-B
1. Discuss the role of phospholipid, cholesterol and carbohydrates in the structural and functional aspect of plasma membrane. [2016-S]
2. State different types of transport of molecule across biomembrane. Mention charecterestics of Carrier Mediated Transport. Differentiate between primary active transport with that of secondary active transport.[2+2+3][2019-S]
GROUP-C [SHORT NOTE]
1. Receptor mediated endocytosis[2014]
2. Ionophores [2014]
3. Secondary active transport [2017-S]
GROUP-D[EQ]
1. Colloids are biologically important having clinical significance.[2013]
2.Oral Rehydration Solution contains glucose.[2019]
CARBOHYDRATE CHEMISTRY- DIGESTION & ABSORPTION
GROUP-B
1. Indicate in details the chemical composition of glycosaminoglycans and proteoglycans. Name the carbohydrates present in glycopreoteins and glycolipids.[5+2][’13, ‘15]
2. Describe how monosaccharides and amino acids are absorbed from gut.[2014-S,2016-S]
3. Classify polysaccharides. Indicate the structural and functional aspect of each of them[2016-S]
4. Describe the various forms of isomerism exhibited by carbohydrates. Name the carbohydrates present in glycoproteins.[5+2][2017]
5. Describe the different types of bond present in heterogeneous polysaccharides with example. [2017-S]
6. Write down the oxidative phase of HMP shunt pathway & its importance.[6+1][2019-S]
GROUP-C [SN]
1. Blood group antigen.[’10,’16]
2. Glycemic index[‘17]
3. Invert sugar[‘17]
4. Glucose transporter[‘17]
5. Composition and function of hyaluronic acid[2017-S]
6. Discuss isomerism of glucose. [2018-S]
7. Glycosaminology [‘19]
8. Glycosides [2019-S]
9. RBC Group Antigen[2019-S]
GROUP-D [EQ]
1. Glucose and fructose form similar osazone crystals.[2011, 2018]
2. Defective lactose digestion may lead to a clinical condition.[2015]
3. Hyperurecemia occurs in Von-Gierke disease.[2018]
4. Thiamine deficiency is detected by measuring transketolase activity in blood’[2018]
5. Benedict test is used to identify reducing sugar.[2018-S]
LIPID CHEMISTRY-DIGESTION & ABSORPTION
GROUP-A
1. Classify phospholipids with examples. Mention their specific role in maintaining the fluidity of plasma membrane. [10+2][2013, 2010-S 7 marks, 2018 7 marks]
2. Name the membrane phospholipids. Draw the structure of lecithin. Write the products formed by the action of different types phospholipases on lecithin. State the physiological role of lysophospholipids & fatty acids produced by the breakdown of lecithin.[3+1+4+4][2019-S]
GROUP-B
1. Tabulate a detailed account of chemical composition of plasma lipoproteins.[7][2010]
2. Classify the fatty acids in details & indicate their physical properties.[5+2][2010-S, 2017]
3. Indicate the chemical composition and methods of separation of plasma lipoproteins. [2017-S]
4. Name ketones bodies. Outline the steps of synthesis & utilization of ketone bodies.[1+6][2019-S]
GROUP-C [SHORT NOTE]
1. Separation & identification of lipid by thin layer chromatography[‘13]
2. Omega-3fattyacids.[2015]
3. Glycosphingolipids[2017]
4. Sialic Acid [2017-S]
5. Plasmalogens [2017-S]
6. Sphingomyelin[2018-S]
7. Ecosanoids[2019]
8. Phospholipase [2019-S]
GROUP-D[EQ]
1. Arachidonic acid may not be considered as an essential fatty acid.[2010]
2. Lecithin is amphipathic as well as amphoteric in nature.[2014]
3. Acid number helps in the identification of rancidity in fats and oils.[2016]
4. Apolipoprotein is a ligand for cell rexeptors.[2016-S]
5. Trans fatty acid is injurious to health.[2018-S]
6. Dipalmitoyllecithin acts as surfactant of alveolar fluids[2019]
7. Cholesterol is essential for digestion of lipids[2021]
PROTEIN CHEMISTRY-AMINO ACIDS, HEMOGLOBIN
GROUP-A
1. Discuss the four orders of protein structures. Describe the alpha helical form of a globular protein. State briefly how the amino acid sequence in a polypeptide chain can be determined.[6+2+4][2010]
2. Discuss briefly how the chemical structures of myoglobin and hemoglobin influence their biological activities. Describe the changes that take place in hemoglobin on oxygenation.[6+6][2010]
3. Describe the peptide bond. What are the different forces that stabilize the protein ,structure at the different levels of organization? Give an example to explain the primary structure that determines the functional state of proteins.[4+5+3][2011]
4. Describe how the amino acid composition, N-terminal & C-terminal residues of a protein are determined & identified. Describe the bonds
responsible for the four structures of proteins. Briefly indicate how a molecular weight of a protein is determined.[7+3+2][2013]
5. Describe the salient features of alpha helix and beta pleated sheet structure of proteins. Mention the non-covalent interactions which stabilize protein confirmation. Briefly discuss the role of peripheral & integral proteins in the network of plasma proteins.[4+3+5][2014]
6. Compare and explain the oxygen binding curves of hemoglobin and myoglobin. Indicate the conformational changes that occur in hemoglobin on oxygenation.
Mention the basic variations in the chemical structures of HbS and HbM as compared to the adult hemoglobin.[6+3+3][2014][2016]
7. Describe the bonds responsible to mention the four orders of protein structure. Describe the physical methods by which the molecular weight of a protein can be determined. Explain how a polypeptide can be synthesized to in the laboratory[6+4+2] [2017-S]
8. Describe in detail how the number, kind and sequence of amino acids in a polypeptide chain are determined.[4+4+4]
9. Describe the methods of determination of primary structure of proteins. [2018]
10. Classify protein on the basis of their biological function and give one example of each protein. Compare and contrast the structure of keratin, myoglobin and haemoglobin. Draw O2 dissociation curve of HbA (adult haemoglobin) and HbF (foetal haemoglobin) and explain the difference between them.[3+6+3][2019]
11. Write down different levels of organization of protein. Write down the steps of haem degradation.{5+5][2021]
GROUP-B
1. Describe the principles of electrophoresis. Illustrate with diagram the electrophoretic separation of the serum proteins indicating the significance of each separated band. Explain the importance of acute phase reactants. [3+2+2][2014]
2. Classify L-amino acids present in the proteins. Explain how amino acids are separated and identified from a mixture of amino acids. [2+5][2015]
3. Write down the synthesis of bilirubin. Explain the term direct bilirubin, indirect bilirubin and Van der Berg reagent. Mention the changes that take places in serum bilirubin (direct) and bilirubin(indirect) level in haemolytic and obstructive jaundice.[4+2+1][2019]
4. Outline the process of synthesis of ammonia in human system. Stae different routes of disposal of ammonia from human body.[4+3][2019-S]
GROUP-C[SN]
1. Glycosylated Hemoglobin.[2011, 2018]
2. Prions.[2011]
3. Selenocystine.[2015]
4. Beta pleated sheet.[2017]
5. Classification of amino acid[2018-S]
6. Discuss secondary structure of protein[2018-S]
7. Peptide bond[2019-S]
GROUP-D[EQ]
1. 2,3BPG helps in delivery of Oxygen to the tissues.[2011]
2. Glycine solution cannot rotate the plane of plain polarized light.[2012]
3. Patient with Hb-S often suffers from anemia.[2013][2017]
4. Myoglobin does not exhibit Bohr effect.[2015]
5. Chaperons play a very significant role in protein folding.[2016, 2018]
6. Hb-A1c provides valuable information for management of diabetes mellitus.[2016]
7. HbF has more affinity towards oxygen than HbA.[2019-S]
8. Hemoglobin is supposed to have all four levels of protein structure.[2021]
ENZYMES
GROUP-A
1. Explain the Michaelis Menten equation and explain the role of substrate concentration on the rate of enzyme catalyzed react ion with the help of graphs. Illustrate how Vmax and Km are affected by competitive and non-competitive inhibition of enzymes. “The Km value for glucokinase is much higher than that for hexokinase though both act on glucose” explain the statement.[6+4+2][2017][2013]
2. Name 5 enzymes whose catalytic activities are altered by covalent phosphorylation-dephosphorylation and indicate their functions. According to International Union of Biochemists, enzymes are classified into six major groups. Indicate in which groups the following enzymes belong: i)Adenylatecyclase, ii)DNA dependant RNA polymerase. iii)Aldolase, iv)Chymotrypsin, v)Reverse Transcriptase, vi)Enolase vii)Acetyl CoA carboxylase.[5+7][2017][2015]
3. Describe different types of enzyme inhibition. Write the clinical importance of enzyme inhibitors.[8+4] [2018]
4. a) State the class in which the following enzyme do belong:
i) Acetylcarboxylase. ii)Fumarase iii)Phosphoglucomutase. iv)Aldolase. V)pepsin vi)RestrictionEndonuclease.
b)Classify the regulatory enzyme. Explain the process of covalent regulation of rate limiting enzyme with suitable example.
c) State at least one pathological condition with rise in activity of the following enzymes in blood: i)SGPT ii)Alkaline Phosphatase. iii)Amylase. iv)RBC Transketolase. v)Creatine phosphokinase. vi)LDH[3+6+3][2019]
5. A) State atleast one pathological condition which increase the activity of following enzyme in blood: Lipase, CPK-MB, RBC glutathione reductase, SGOT
B) Explain with the help of enzyme velocity curve how following factors regulate the enzyme activity: Concentration of enzyme, Concentration of substrate, pH, Temperature. [4+8][2019-S]
6. Classify enzymes according to IUB with example of each. Differentiate between the lock and key model & induced fit model for enzyme catalysis. What factors effect enzyme activity. Briefly discuss different mechanism of enzyme inhibition. [6+3+2+4][2021]
GROUP-B
1. Define isoenzymes. Write the clinical significance of serum isoenzymes in cardiac disorder.[2+5][2012-S]
2. Describe in details hpw covalent modification and repression/depression mechanism can regulate the enzyme action in vivo.[7][2014-S]
3. Explain the mechanism of allosteric regulation of enzyme activity using PFK as an example. Mention the other mechanisms by which the enzyme action is regulated.[4+3][2016]
4. Describe the oxido-reductase group of enzymes. [2018]
GROUP-C[SN]
1. Km of enzyme[2012-S]
2. Co-enzyme[2012-S]
3. Ribozyme [2014-S][2016-S][2018]
4. Non-functional enzyme[2016]
5. Michalis-Menten equation[2016-S]
6. Isoenzyme [2018-S]
GROUP-D[EQ]
1. The mode of action of metallo-enzymes and metal activated enzymes are different.[2013]
2. Isoenzymes of Alkaline Phosphatase are of diagnostic significance.[2014]
3. Nonfunction plasma enzymes are important only for clinical purposes.[2014]
4. Methotrexate is a competitive enzyme inhibitor.[2014-S]
5. Apolipoproteins are enzyme cofactors.[2014-S]
6. In competitive inhibition, larger amount of substrate can overcome the effect of inhibition.[2014-S]
7. Isoenzyme assay is helpful in the diagnosis of MI.[2015]
8. Metalloenzymes and metal activated enzymes are not similar. [2016-S]
9. Allopurinol is called suicide inhibitor.[2018-S]
10. Coenzymes act as co-substrate in the enzyme catalyzed reaction.[2019]
CARBOHYDRATE METABOLISM
GROUP-A
1. Describe in a flow diagram the metabolic pathways of glycogen formation and degradation in the body. Describe in separate chart show cyclic AMP regulates this process by enzyme modification. [4+8][2013]
2. In a flow diagram describe the metabolic steps of glycogenesis and glycogenolysis in muscle and show how cAMP integrates their regulation.[6+6][2010,2018-S]
3. Describe the metabolic steps of citric acid cycle in a flow diagram indicating the enzymes and co-enzymes involved and highlighting the steps where the energy is produced. Mention the steps in the cycle which are irreversible in nature. Indicate how propionate is converted to one of the intermediates of this cycle.[8+2+2][2013]
4. In a flow diagram ,indicate the metabolic steps by which propionate can be converted to glucose and show how key enzymes of gluconeogenesis are controlled.[6+6][2010]
5. On complete oxidation, glucose leads to production of carbondioxide and water. Mention those metabolic steps where carbondioxides are evolved. Give a detailed account of enzymes, co-enzymes and control mechanisms involved in these steps. Mention three examples of metabolic reactions where carbon dioxide is utilized in this process.[6+3+3][2016]
6. Describe in detail how glycogenic amino acids are converted into glucose in the body by TCA cycle and reverse pathway of glycolysis. [2016-S]
7. Describe the role of insulin and glucagon on gluconeogenesis process in fed and starved state. [2018-S]
8. Describe differences between the anaerobic and aerobic pathways of glycolysis. Explain how RBCs can continue glycolysis without any synthesis of ATP’ Explain how metabolic pathway of galactose and fructose are linked to glycolytic pathway.[6+3+3+3][2021]
GROUP-B
1. Describe multi-enzyme complex and various reactions involved in the oxidation of pyruvic acid to acetyl-CoA.[7][2011]
2. Describe the process of formation of glucose from lactate indicating the regulatory steps.[4+3][2012-S, 2018]
3. Describe in details how pyruvate is converted to Acetyl-CoA in the body.[7][2013].
4. Give a brief account of glycogen storage disease.[7][2014].
5. Describe the hormonal control of glycogenesis and glycogenolysis in a flow diagram. [2016-S]
6. Explain with a flow diagram how glycolysis and gluconeogenesis in the liver are controlled by fructose 2,6 bis phosphate & the bifunctional enzyme6-phosphofructo-2-kinase.[7][2017]
7. With flow diagrams, indicates the normal and abnormal metabolism of fructose and galactose the body.[7][2017-S]
8. Write down the non-oxidative process of HMPShunt Pathway and it’s importance.[6+1][2019]
GROUP-C[SN]
1. Rapoport Leuberin cycle[’11,’17]
2. Essential Pentosuria [’10,’16]
3. Pyruvate dehydrogenase [‘19]
GROUP-D[EQ]
1. Long chain fatty acids cannot be converted to glucose in human body though the reverse is possible.[2010]
2. Impairment of pentose phosphate pathway(PPP) leads to erythrocytic hemolysis.[2011]
3. Phosphofructokinase-I is known as pacemaker of glycolysis.[2012]
4. Von-Gierke’s disease is associated with hyperuricemia.[2012][2017]
5. G6PD deficiency develops anemia.[2012-S][2017-S]
6. Fat can be synthesized from glucose but glucose can’t be synthesized from fat.[2016]
7. Galactosemic patients are often associated with congenital cataract.[2016]
8. Uncontrolled DM causes cataract. [2018-S]
LIPID METABOLISM
GROUP-A
1. Give an account of fatty acid synthase complex. Describe the metabolic pathway for de-novo synthesis of palmitate in the body.[3+9][2014]
2. Describe the metabolic steps of biosynthesis of cholesterol.Discuss the control metabolism associated with HMG CoA reductase. Explain reverse cholesterol transport.[8+2+2][2017]
3. Describe how palmitic acid is oxidised in the body completely and calculate it’s net gain in energy. Explain how the complete oxidation of oleic acid different from that of palmitic acid.[8+2+2] [2017-S]
4. Write the metabolism of VLDL. Explain the reverse-cholesterol transport. [8+4][2018]
5. Write down the steps of beta-oxidation of fatty acid. Why defective beta oxidation may lead to hypoglycemia.[6+4][2021]
GROUP-B
1. Give the exact chemical composition of very low density lipoprotein. Explain their formation and fate inside the body.[2+5][2013]
2. Describe how ketone bodies are formed & subsequently degraded in the body.[3+4][2015]
3. Describe with the help of a diagram digestion of a triglyceride and it’s absorption from intestine, with special reference to the role of bile in the process.[2019]
4.Write down the β-oxidation of palmitic acid and mention problem that arise out of medium chain Acyl CoA Dehydrogenase deficiency.[6+1][2019]
GROUP-C[SN]
1. Control of HMG-CoA reductase.[2013]
2. Role of carnitine in fatty acid metabolism.[2015]
3. Fatty acid synthase complex.[2017]
4. Fatty liver[2017-S]
GROUP-D[EQ]
1. Statin group of drugs(atorvastatin) act as cholesterol lowering agent.[2012-S, 2019-S]
2. Ketone bodies are degraded in the extra hepatic tissues only.[2013]
3. Both uncontrolled diabetes mellitus and prolonged fasting produce ketosis but its magnitude is less in the case of prolonged fasting.[2014]
4. HDL is involved in reverse cholesterol transport.[2015, 2019]
5. Lipoprotein lipase deficiency may lead to hyperglyceridemia.[2015]
6. Consumption of alcohol leads to fatty liver.[2015-S, 2016-S]
7. Citrate plays an important role in fatty acid synthesis.[2017, 2018-S]
8. Increase intake of fructose leads to formation of more VLDL.[2017-S]
9. Ketone bodies are not waste material. [2018-S]
10. HDL C is good cholesterol.[2018-S]
PROTEIN METABOLISM
GROUP-A
1. Name the aromatic amino acids. Outline the catabolic pathway of phenylalanine mentioning the disorders relating to that.[Describe how catabolism of haem produces bilirubin. Indicate in details the process of uptake, conjugation and secretion involved in transfer of bilirubin from blood to bile.[6+6][2014]
2. Discuss an essay on biosynthesis of urea. How it is regulated. Add a note on the clinical significance of uremia. [2018-S]
3. Describe the reaction of transamination and oxidative deamination of amino acids in the body. What are the effects of hyperammonemia?[3+3+4][2021]
GROUP-B
1. Describe how catecholamines are synthesized and degraded inside the human body.[3+4][2010]
2. Write the synthesis, transport and degradation of catecholamines.[7][2011]
3. Describe the process of transamination and oxidative deamination in the body.[4+3][2014]
4. Explain the role of glutamic acid in removal of ammonia from amino acid. Why ammonia is toxic to central nervous system. [2018]
GROUP-C[SN]
1. Maple Syrup Urine Disease.[2010]
2. Polyamines.[2010]
3. S-Adenosyl Methionine.[2013]
4. Acute intermittent porphyria.[2014]
5. Phenylketonuria [2016-S, 2018-S, 2019-S]
6. Hyperbilirubinemia [2016-S, 2018]
7. Oxidative & non-oxidative deamination. [2017-S]
8. Alkaptonuria [2019]
9. Transmethylation [2019-S]
GROUP-D[EQ]
1. Urine turns black on standing in Alkaptonuria.[2010]
2. Phototherapy (exposure to blue light) helps in treatment of neonatal Physiological jaundice.[2011][2017-S]
3. Ammonia is toxic to Central Nervous System.[2012, 2016-S]
4. Patient with carcinoid syndrome may exhibit pellagra.[2013]
5. Alkaptonuria is often associated with generalized pigmentation of Connective tissue (Ochronosis).[2013]
6. Drugs may precipitate attacks of porphyria in some patients. [2017-S]
7. Hartnup disease gives rise to pellagra like syndrome.[2019]
8. Hemoglobin is supposed to have all four levels of protein structure.[2021]
BIOLOGICAL OXIDATION
GROUP-A
1. Describe all the complexes with their components of the respiratory chain in mitochondria with the probable sites of ATP synthesis. Indicate the names of different inhibitors with their sites of inhibition. Name some uncouplers associated with respiratory chain and indicate their significance.[8+2+2][2014-S, 2018]
2. Describe the organisation of electron transport chain mentioning the components of all four complexes and the reaction catelised by them. Explain the mechanism of ATP synthesis in the mitochondria by ATP synthase. [2016-S]
GROUP-B
1. Describe the chemiosmotic coupling hypothesis of oxidative phosphorylation.[7][2010]
2. Describe the mitochondrial electron transport chain. How the inhibitors of ETC differ from uncouplers of oxidative phosphrylation?[5+2][2011]
3. Describe the operation and significance of glycerophosphate shuttle and malate shuttle.[3+4][2014]
4. What is oxidative phosphorylation? Differentiate it from substrate level phosphorylation. Illustrate with a diagram how ATP is synthesized in mitochondria?[2+2+3][2014]
5. Name the components of the electron transport chain with the help of a diagram. Explain how the electron flows from the NADH+H+ to the molecular oxygen through the different components of ETC.[2+5][2019-S]
GROUP-C[SN]
1. Uncoupler of oxidative phosphorylation.[2019]
GROUP-D[EQ]
1. Brown adipose tissue promotes thermogenesis.[2011,‘10]
2. G6PD is responsible for erythrocyte membrane rigidity.[2014]
3. Brown fat is responsible for non-shivering , genesis in newborn. [2016-S]
4. F0F1 ATPase give rise to ATP synthesis in intact mitochondria.[2019-S]
5. TCA is known as amphibolic pathway.[2021]
ACID-BASE BALANCE
GROUP-A
1. Describe in detail how pH of the blood is regulated by lung and kidney. Give an account of metabolic acidosis and anion gap.[4+4+2+2][2014-S, 2018-S]
GROUP-B
1. Describe the renal mechanism for regulation of acid base balance.
2. What is the biomedical importance of anion gap?[4+3][2014]
3. Name the blood buffers. Explain the role of blood buffers in the maintenance of normal pH of blood.[2019]
4. Write down the Henderson Hasselbalch equation. Explain the role of kidney in the maintenance of acid base balance in our body.[1+6][2019-S]
GROUP-C[SN]
1. Respiratory acidosis[2013]
2. Henderson – Hasselbach equation [2013-S]
3. Alkali reserve[2018]
4. Bicarbonate buffer system[2021]
GROUP-D[EQ]
1. Cellular exchange of ion maintains hydrogen ion homeostasis. [2017-S]
FUNCTIONAL TEST
GROUP-B
1. Describe the methods of determining the chemical structure of any unknown biomolecule.[7][2017]
2. Describe the principles of different forms of chromatography and indicate their role in clinical diagnosis. [2017-S]
3. Enumerate the difference between autosomal dominant and recessive disorders giving examples. [2017-S]
GROUP-C[SN]
1. Electrophoresis.[2016, 2018-S]
2. Ion exchange chromatography. [2016-S]
3. Enzyme assay by coupling to a dehydrogenase[2016-S]
4. Abnormalities of thyroid function.[2018-S]
5. Biochemical function of ascorbic acuid.[2018-S]
6. Thin Layer Chromatography.[2019-S]
GROUP-D[EQ]
1. Renal clearance study is a nearly predictor of impending renal failure.[2014, 2018]
2. Levels of hepatic enzymes can differentiate b/w hemolytic, hepatocellular and obstructive jaundice.[2013]
3. Urinary urobilinogen is increased in hemolytic jaundice. [2018]
4. Phototherapy is better alternative than Phenobarbital in treatment of Crigler Najjar syndrome type I.[2021]
FREE RADICALS, ANTIOXIDANTS & XENOBIOTICS
GROUP-B
1. Explain the different phases of metabolism of xenobiotics. [7][2016-S]
GROUP-C[SN]
1. Super-oxidedismutase.[2013]
2. Role of Cyt-P450 in hydroxylation reaction.[2013]
3. Lipid peroxidation reaction [2013-S][2016-S]
4. Biochemical functions of peroxisomes.[2014]
5. Antioxidant enzymes.[2014]
6. Reactive oxygen species[2019]
7. Cyt-P450[2014-S, 2019]
8. Phase II reaction of Xenobiotics.[2019-S]
GROUP-D[EQ]
1. Glutathione plays a vital role in detoxification. [2016-S]
2. Hydroxylation reactions often require the presence of ascorbic acid. [2017-S]
3. Macrophages shows beneficial effects by generating free radicals.[2021]
VITAMIN, MINERALS & NUTRITION
GROUP-A
1. What is a balanced diet? What is the nutritional importance of dietary proteins? Discuss the protein energy malnutrition with special reference to kwashiorkor disease.[3+6+6][2021]
GROUP-B
1. Indicate the factors which modified absorption of calcium from the gut. Discuss in detail how calcium metabolism is controlled by calcitriol and parathyroid hormone. Enumerate the biochemical role of intracellular calcium.[3+4] [2016-S]
GROUP-C[SN]
1. Folic acid as coenzyme[2016-S]
2. Folate trap[2018]
3. Nitric oxide having various role.[2018-S]
4. Biochemical function of ascorbic acid[2018-S]
GROUP-D[EQ]
1. Transamination reaction cannot take place without pyridoxine.[2017-S]
2. Vitamine K deficiency is responsible for haemorrhage disease of newborn.[2019]
3. Normal function of the kidney is essential for the synthesis of active Vitamin D3.[2019-S]
4. Deficiency of ascorbic acid causes fragility of blood vessels.[2021]
NUCLEOTIDE CHEMISTRY
GROUP-A
1. Describe the Watson Crick model of DNA structures enumerating its salient features. Explain the role of Histone Protein in the organisation of DNA. Indeed gate how denaturation of DNA is used to analyse its structure. [2016-S]
GROUP-B
1. Indicate the functional aspect of all varieties of RNA. [2016-S]
2. Describe Watson crick model of DNA structure. Draw and label structure of tRNA[4+3] [2018-S]
GROUP-C[SN]
1. t-RNA[2011]
2. Bonds in polynucleotides.[2017]
3. sn RNA, mi RNA, si RNA [2017-S]
4. Melting of DNA [2018]
GROUP-D[EQ]
1. RNA is alkali labile while DNA is alkali resistant.[2012, 2013-S, 2019-S]
2. DNA with higher GC content have relatively higher Tm.[2014]
3. Synthetic nucleotides are used as drugs.[2015]
4. DNA is more stable than RNA.[2016]
5. Adenine nucleotides have various functions beside making nucleic acids.[2017]
6. Nucleotide analogs are used as anticancer agents.[2018]
NUCLEOTIDE METABOLISM
GROUP-C[SN]
1. Gout.[2013]
2. Source of nitrogen and carbon atoms of the purine ring.[2013]
3. Purine Salvage Pathway.[2018]
GROUP-D[EQ]
1. Synthetic nucleotides are used as drugs.[2015]
2. Intake of alcohol may aggravate the symptoms of gout.[2016]
3. Allopurinol lowers the uric acid concentration of blood.[2012-S, 2019]
4. Gout is precipitated by alcohol intake.[2012-S, 2016-S, 2018-S, 2021]
MOLECULAR BIOLOGY & GENETICS
GROUP-A
1. Describe the stage of initiation of translation process with the help of a diagram. State the mechanism of action of the following antibiotics in the inhibition of translation: A) Streptomycin, B) Erythromycin, C) Chloramphenicol.[6+6][2011]
2. Write down the different types of DNA damage. Explain the mechanisms of: Mismatch DNA repair, Base excision repair, Nucleotide excision repair.[6+6][2011]
3. Define operon. Describe the Lac-operon model for regulation of gene expression in E.Coli.[2+10] [2018]
4. Write with the help of a diagram, describe the stage of initiation and elongation of translation process in E.coli. State the mechanism of streptomycin and puromycin in the inhibition of translation process on prokaryotes.[9+3][2019]
5. Write down with the help of a diagram stage of initation and elongation of replication process. Differentiate between DNA polymerase I and DNA polymerase III[3+9][2019]
6. Name the different types of DNA damage. Mention different types of DNA repair. With the help of diagram differentiate between ‘Mismatch repair’ & ‘Base Excision Repair’[2+2+8][2019-S]
7. With the help of asuitable diagram explain the ‘Lac-operon model’ of regulation of gene expression in bacteria. Differentiate between the mono-cistronic & poly-cistronic mRNA.[10+2][2019-S]
8. Explain replication of a DNA molecule in the context of initiation, elongation and termination in prokaryotes with suitable diagrams. Enumerate the difference b/w DNA polymerase I, II & III.[10+5][2021]
GROUP-B
1. Describe how ribonucleic acid is synthesized. Indicate the difference b/w DNA Polymerase III and RNA polymerase.[5+2][2010]
2. Describe the initiation, elongation and termination phase of transcription in eukaryotes. Name the antibiotics which specifically inhibit the microbial protein synthesis.[5+2][2015-12marks][2013]
3. Enumerate different types of DNA repair.[7][2015-S, 2018]
4. Give an account of negative and positive regulation of lac operon in E.Coli.[2015][7]
5. Enumerate the DNA damageing agents and indicate the types of damages made by them.[7][2017]
6. Expand the term PCR. Describe different steps for a PCR reaction. Enumerate any four uses of the PCR.[1+7+2][2021]
7. Enumerate the different modes of repair of DNA damage in humans. Explain the mechanism of any one of them with the disorder arising due to the defects on that pathway.[4+4+2][2021]
GROUP-C[SN]
1. Restriction Fragment Length Polymorphism (RFLP).[2011]
2. Monoclonal antibodies.[2011]
3. Polymerase Chain Reaction.[2012-S, 2015-S. 2018]
4. Base excision repair of DNA.[2013]
5. Frame shift mutation.[2013]
6. Eukaryotic topoisomerase.[2014]
7. Polyclonal antibodies.[2014]
8. Radioisotopes.[2014]
9. DNA replication in eukaryotes and prokaryotes.[2015]
10. RNA editing.[2015]
11. Use of in vitro DNA amplification process in the laboratory[2015-S]
12. Post translational modification of proteins[2015-S]
13. Point mutation.[2012-S,2016]
14. Restriction endonuclese[2017-S]
15. Eukaryotic DNA polymerases[2017-S]
16. Satellite, minisatellite and microsatrllite DNA.[2017-S]
17. Point mutation.[2019]
18. Genome of retrovitus.[2019]
19. Genetic Code.[2019-S]
GROUP-D[EQ]
1. RNA can act as enzyme.[2011]
2. Genetic code is degenerate.[2012-S, 2018]
3. DNA is much more stable than RNA.[2016]
4. Ribosome is the ultimate ribozyme.[2017]
5. Recombinant DNA technology is required for selective amplification of a
6. particular gene.[2017-S]
7. RNA editing mechanism is responsible for APO B48 synthesis in the
8. intestinal cells.[2019]
IMMUNE-CHEMISTRY & CANCER
GROUP-B
1. Draw the representative structure of IgG. Classify immunoglobin and mention the function of each class.[2017-S][2019]
2. Describe the structural characteristics of an Ig molecule in general with a diagram. Explain the functional difference b/w T cell & B cell mediated immunity.[5+5 [2021]
GROUP-C[SN]
1. Cell cycle regulators.[2010]
2. Structure & function of IgG [2011-S][2015-S][2018]
3. Tumor markers.[2012-S, 2014,2016-S, 2021]
4. Ceruloplasmin.[2014]
5. Proto-oncogenes[2014-S][2018]
6. Oncogenes[2016-S]
7. Radio isotope in treatment[2018-S]
8. Cell cycle[2021]
GROUP-D[EQ]
1. Methotrexate is used for anti-cancer therapy.[2012,2011, 2016-S, 2019-
2. S]
3. Radio Immuno Assay techniques has got demerits also.[2013]
4. Telomeric length is maintained in cancer cells and stem cells.[2016-S]
5. P53 is considered as “Guardian of the genome”.[2019-S]
6. Proto oncogenes are regulatory genes[2021]
7. Under some conditions immunity causes damaging effect[2021]
MOLECULAR ENDOCRINOLOGY
GROUP-A
1. Classify hormones according to their mechanism of action. Indicate the structure and function of thyroid hormone. Explain the inhibitor action of iodine and thiocyanate on thyroid function. Explain mechanism inT3 toxicosis [4+4+2+2] [2017-S]
GROUP-B
1. In a flow diagram describe how insulin and glucagon regulate the process of lipogenesis and lipolysis in adipose tissue.[7][2010]
2. Discuss the different types of G-protein coupled signal transduction processes.[7][2010]
3. Explain the mechanisms of signal transductions by cAMP, calcium and phosphatidyl inositol system with the help of diagrams.[7][2013]
GROUP-C[SN]
1. Mode of action of steroid hormone[2010-S]
2. G-Protein[2011]
3. cAMP[2012-S]
4. Insulin receptor.[2019-S]
GROUP-D[EQ]
1. Lipids can act as intracellular signals.[2012]
2. Endocrinal disorder may predispose to obesity.[2021]
EXTRA CELLULAR MATTRIX
GROUP-C[SN]
1. Chemical structure of collagen[2010-S, 2016]
GROUP-D[EQ]
1. Ascorbic acid helps in the maturation of the immune collagen molecule.[2019-S]
