CARBOHYDRATE CHEMISTRY

Short Notes
1. Classify carbohydrates with suitable examples.
2. Mention physiological importance of three hexoses.
3. Name a pentose present in nucleic acid.
4. What are different tests that can be performed with glucose, fructose, lactose maltose? What will
be observation?
5. Explain mutarotation with example.
6. Name two properties of monosaccharide that go along with mutarotation.
7. What are epimers? Ilustrate with two examples.
8. If a aldose sugar contain 3 asymmetric carbon units, how many diastereoisomers are possible?
9. What is the principle of benedicts reaction? What are the components of benedict reagent?
10. How can the presence of a reducing sugar be detected? Give an example of non-reducing sugar and
indicate its source.
11. Describe the osazones of different sugars. What are furfurals.
12. What is milk sugar? What are its components?
13. What is composition of invert sugar. What is its precursor?
14. Explain the term invert sugar and inversion.
15. What are homopolysaccharide. Give two examples.
16. Name the storage polysaccharide of human body. Name the tissue in which it is stored.
17. Explain how glucose molecules are combined together to form glycogen.
18. Name a polysaccharide made up of fructose units.
19. What is biomedical importance of cellulose?
20. Enumerate general features of glycosaminoglycans. List any three glycosaminoglycans & their
functions. Name a heteropolysaccharide that does not contain uronic acid. Name intracellular GAG.
21. Define glycosides. What is cardiac glycoside?

CARBOHYDRATE METABOLISM

Glycolysis

Long Questions:

1. Enumerate the steps of Glycolytic pathway with energetics and mention two inhibitors.
Short Questions:

1. Enlists the steps in glycolysis and give the number of ATPs formed in it from a single
molecule of glucose .
2. Narrate the irreversible steps in glycolysis
3. .What are the regulatory enzymes in glycolytic pathway?
4. Write short notes on glycolysis in RBC.
5. Describe the malate – aspartate shuttle and its significance
6. Explain the digestion and absorption of carbohydrates
7. Write briefly on the Rappaport – Leubering cycle.
8. Why should lactate be the end product of glycolysis in RBC’s? Explain.
9. How does the difference in Km value between glucokinase and hexokinase suits its
functions?
10. Discuss the difference between Hexokinase and Glucokinase.
11. How do you preserve a sample of blood which is meant for blood glucose estimation.
What happens to glucose in an oxalated blood?
12. Write a note on cori’s cycle
13. What is 2,3 bisphosphoglycerate? What is its signifance?
14. Give an example of an allosteric enzyme present in glycolytic pathway.
15. What are the possible fates of glucose – 6 – phosphate in the cell?
16. Formation and Fate of pyruvate

TCA Cycle

Long Questions:

1. Give an outline of citric acid cycle indicating the enzymes, coenzyme and sites of ATP
production. Add a note on its energetic and amphibolic nature.
Short Questions:

1. Why is it called the final common pathway

2. How many ATP’s are produced when one molecule of pyruvate is oxidized fully fully to
CO2 and H2O
3. What is anaplerosis? Give two anaplerotic reactions?
4. Substrate level phosphorylation in TCA.
5. How is pyruvate converted to acetyl Co A
6. Name the coenzymes for Pyruvate dehydrogenase complex.mention its function.
7. Give the reaction catalysed by succinate dehydrogenase. Name the competitive inhibitor
of this enzyme
8. Give the reaction catalysed by enolase. Name one inhibitor for this enzyme. What is its
applied importance?
9. What are the sources of Acetyl CoA formation?
10. Which enzyme in TCA cycle is inhibited by Arsenite?

Gluconeogenesis:

Long Questions

1. Define gluconeogenesis. What are its substrates? Explain the various reactions involved
in this process. What are the clinical and physiological significance of gluconeogenesis?
2. Describe the pathway of conversion of lactate to glucose? Describe the regulation of
Gluconeogenesis.
3. Trace the pathway of Gluconeogenesis. Mention their Key enzymes.
Short Questions:

1. What is the need for gluconeogenesis?

2. Mention a regulatory molecule that reciprocally controls gluconeogenesis and glycolysis
3. How is glycerol converted to glucose?
4. Which steps of glycolysis have to be circumvented during gluconeogenesis? Mention the
enzymes involved.
Glycogen Metabolism

Long Questions

1. Describe in detail the synthesis and breakdown of glycogen. How is it regulated?

2. Describe in detail the synthesis and breakdown of glycogen. How is it regulated?
3. Explain how glucose molecules are combined together to form glycogen.
Short Notes:

Discuss the regulation of glycogen synthase?

Describe the metabolic fate of muscle glycogen during severe muscular exercise?

Why muscle glycogen does not contribute to blood glucose?

HMP Pathway

Long Questions

1. Describe the steps of Embden Meyer Hoff pathway of glucose.

2. Describe in detail the importance of HMP shunt pathway and mention the tissues where the
pathway is active? Briefly outline the steps.
Short Questions:

1. What is the importance of pentose phosphate pathway in our body?

2. Name the reactions in which NADPH is synthesized?
3. Deficiency of G 6 PD leads to hemolysis. Explain.
4. Which hexose mono phosphate shunt enzyme has diminished activity in thiamine deficiency?

Diabetes Mellitus

1. Write a note on diabetes mellitus

2. How is insulin secreted? What are the functions in the body?
3. What are the chronic complications of diabetes mellitus?
4. Write a short note on HbA1C and its significance
5. What are the diagnostic criteria for diabetes mellitus?
6. What is glycosuria. State two clinical conditions in which glycosuria is present.
7. C peptide and its diagnostic utility
8. While treating hyperglycemia in diabetic person why K + is added to insulin infusion?
9. Why is ketoacidosis not usually associated with Type -II Diabetes mellitus?
10. Write a note on Glucose Tolerance Test (GTT)

Fructose, galactose, lactose, uronic acid…& Alcohol

1. What are the enzyme defects that can occur in fructose metabolism? Mention the congenital
disorders& enzyme defects in fructose metabolism. (2)
2. What are the urine findings in different types of fructose metabolism? (2)
3. Give two functions of the uronic acid pathway. (1)
4. What are the possible reducing sugars that can be detected in the urine of a newborn? (1)
5. State the enzyme deficient in classical galactosemia? What is the mechanism of cataract
formation in this condition?
6. Which enzyme deficiency leads to lactose intolerance (1)
7. Explain the glucose transportation in various tissues. (2)
8. Essential Pentosuria (2)
9. Mention two important biochemical changes seen in Von-Gierke’s disease. What is the
enzymatic defect?

LIPID CHEMISTRY
1. What are fatty acids? Classify them. Comment on number of carbon atoms in its structure.
2. What is the number of double bonds in arachidonic acid? What are their positions? What is their
biological role?
3. What are prostaglandins? Discuss biological actions and importance and clinical applications of
prostaglandins.
4. What is difference between prostacyclins and thromboxanes?
5. Name unsaturated fatty acids with two double bonds. Mention the position of the double bonds.
6. What are omega 3 fatty acids and their importance?
7. Does trans isomer of oleic acid have a higher or lower melting point than cis-oleic acid? Explain.
8. What is iodine number? Give its significance. What is saponification?
9. What is autoxidation of PUFA known as? Give an example for in vivo antioxidant.
10. What is lipid peroxidation & what is its effect on biological system?
11. Name essential fatty acids. Draw their structure.
12. Classify compound lipids giving examples.
13. Name five phospholipids. Give one function for each. State role of liposomes in therapy.
14. Mention the different components of lecithin. What is significance of L:S ratio?
15. What is the structural feature of Sphingomyelin which enables it to participate in formation of
biomembrane?
16. Cardiolipin
17. Ceramide
18. Membrane lipids are rich in unsaturated fatty acids whereas the storage lipids are rich in saturated
fatty acids. Explain the biological significance and bio -chemical basis of the above two observations.
(5)
19. What is liposome? Mention its application.
20. Give an example of derived lipid.
21. Draw structure of cholesterol. What is its hydrophilic end? Enumerate its functions.
22. Define sterol. Give two examples.

LIPID METABOLISM

Beta-Oxiation of Fatty Acids

Long Questions
1. Describe the β – oxidation of palmitic acid. Add a note on energetics of palmitic acid
oxidation. How is pathway regulated?
Short Questions
1. Calculate the number of ATP’s formed during the complete oxidation of palmitic acid
 2. Omega Oxidation
3. What is beta oxidation of fatty acids? Give its energetic.
4. What is carnitine? Mention its functions
5. How is long chain acyl CoA transported to the mitochondria? What the deficiency of the
transporter lead to?
6. Disorders of fatty acid oxidation
7. What is the fate of Propionyl CoA in oxidation of odd chain fatty acids?
8. Define , β and peroxismal oxidation of fatty acids
9. Refsums disease
10. What are the end products of metabolism of odd chain fatty acids

Explain Briefly
1. Why does b - oxidation of fatty acid does not take place in RBC? (1)
2. Can a fatty acid with even carbon atoms be converted to glucose? (1)
3. Explain why odd chain fatty acids are both ketogenic and glucogenic? (2)
4. What is the role of vitamin B12 in the metabolism of odd chain fatty acid? (2)

Fatty Acid Biosynthesis

Long Question
1. Give an account of extra mitochondrial fatty acid synthesis. Add a note on its regulation
Short questions
1. Regulation of fatty acid synthesis
2. What is the role of the TCA Cycle in providing substrate for fatty acid synthesis in cytosol? (2)
3. Name the major regulatory enzyme of lipogenesis. Mention the activator for this enzyme. (2)

Lipoprotein Metabolism
1. How dietary triglycerides are absorbed and transported in the plasma?
2. Classify lipoprotein. Explain the role of lipoprotein in the transport of lipids.
3. Indicate the basic structure of a lipoprotein. Explain the metabolism of lipoprotein
concerned with the transport of dietary triglycerides.
4. HDL cycle
5. What is reverse cholesterol transport
6. Give the composition and function of chylomicrons
7. What are lipoproteins. What is bad cholesterol? Discuss its clinical significance?
8. Name the lipoprotein synthesized by the intestinal cell (1)
9. A patient was found to have low HDL cholesterol and high LDL cholesterol. What is the clinical
significance of these findings? (1)
10. Draw the general structure of lipoprotein. (2)
11. Why does plasma appear milky after a fat rich meal? Name the enzyme responsible for its
clearance. (2)
12. How do the dietary lipids enter the circulation? (2)
13. Write in detail the significance of apolipoprotein in LDL metabolism. (2)
14. Write briefly about absorption and transport of dietary lipids? (5)
15. How are dietary triglycerides absorbed and transported in the plasma? Explain briefly the
transport of dietary triglycerides from intestine to liver (8)
16. Write the enzyme associated with HDL. (1)
17. Define Lipoprotein. Write in detail about formation, metabolism and clearance of VLDL. (8)
Cholesterol Metabolism & Bile Salts
Long Question
1. Describe the synthesis and degradation of cholesterol. Add a note on its regulation.
2. Regulation of cholesterol biosynthesis
3. Name the regulatory enzymes in cholesterol synthesis. Name two inhibitors of this
enzymes.
4. What are the byproducts of cholesterol. What are its excretory products?
5. Give the normal values of serum cholesterol and one pathological condition in which it is
altered
6. Name the common precursor for all steroid hormones. From which biochemical
substances steroid hormones are formed
7. Which is the rate-limiting enzyme in cholesterol biosynthesis? (1)
8. Name the biologically important compounds derived from cholesterol. What is the normal level of
cholesterol in plasma? (2)
9. How does the cholesterol influence the membrane property by its presence? (2)
10. How is HMG CoA formed and utilized? (2)
11. How statin group of drugs lowers plasma cholesterol? (1)
12. Name the ring structure in cholesterol and the compounds formed from cholesterol.
13. Add a note on familial hypercholesterolemia.(8)
14. Causes and investigation in a case of hypercholesterolemia.(MD)
15. What is the role of cholestyramines resin in bile acid metabolism? (2)
16. What is enterohepatic circulation of bile salts? (5)
17. Name the secondary bile acids. (1)
18. Formation and uses of bile acids (5)
19. Name the two primary bile acids. (1)

20. Name the primary and secondary bile acids. What are their functions?

Ketone Bodies
Short questions
1. Explain the biosynthesis and utilization of Ketone bodies
2. Describe the steps involved in ketone body production.
3. Write a short note on ketosis
4. Name the ketone bodies. Mention the test to detect ketone bodies in urine.
5. Why ketone bodies cannot be used as a fuel by the liver? (1)
6. What is the site of formation of acetoacetate from fatty acids? (1)
7. Name the ketone bodies excreted in urine and explain Rothera’s test (2)

Digestion & Absorbtion of lipids

Short notes
1. Digestion and absorption of lipids
2. How are fats mobilized from adipose tissue and what is the fate of products formed
3. What is steatorrhoea? What are the causes of steatorrhoea?
4. Role of pancreatic juice in digestion
Adipose tissues
Short notes
1. What is the major function of adipose tissue? Mention the major pathway, the main substrates
and products in the adipose tissues (2)
2. What is thermogenin? State its role in fat storage (2)

Eicosanoids
Short notes
1. Functions of Eicosanoids
2. Enumerate the clinical applications of prostaglandins
3. Name the steps in prostaglandin synthesis. Name one inhibitor of this pathway. (2)
4. Explain the biochemical basis by which aspirin and indomethacin carry out their anti-inflammatory
actions.(1)
5. What are Eicosanoids?(1)

Fatty Liver & Clinical

Short notes
1. What is fatty liver? Explain its causes. Add a note on lipotropic agents.
2. Describe lipid profile and its clinical importance.
3. Name any four lipid storage disease and mention the defect in them
4. What is Niemann –Picks disease due to? Give any two of its clinical features.
5. Name any six risk factors for the development of Atherosclerosis.
6. Lipid storage disorders
7. Discuss the role of liver in the metabolism of lipids.
8. Give examples for dietary fibres and mention the beneficial effects of dietary fibre. (2)
9. Why marine lipids are preferred to vegetable oils in the dietary management of coronary heart
diseases? (2)

AMINO ACIDS & PROTEIN CHEMISTRY

Long questions
1. Define structural organization of protein with suitable example. Name a protein that is rich in
alpha helix.
2. What are the forces that stabilize secondary structure of proteins?
Short Questions
1. Name the ketogenic amino acids.
2. Give an example each for amino acids with non-polar side chains and amino acids with ionizable side
chains.
3. How many asymmetric carbon atoms are there in glycine?
4. Name the functional group in histidine.
5. Which primary amino acid is, strictly, not an amino acid? R H
6. Define iso-electric pH. What is its significance?
7. Define pI. Mention any one property of protein at its isoelectric pH.
8. Name the amino acid which has maximum buffering capacity at physiological pH.
9. What are essential amino acids. Name any four of them.
10. Name three important biological peptides and constituent amino acids and functions (Vasopressin,
GSH).
11. Name the protein color reactions answered by glutathione.
12. Name inhibitory neurotransmitter synthesized from amino acid.
13. Write a note on aspartame.
14. Give two examples of non-protein amino acids.
15. What are various function of proteins.
16. Classify proteins based on their functions with suitable examples.
17. Give two examples of zinc metalloprotein.
18. Explain denaturation of protein. Give two causes and two consequences of denaturation.
19. Name two disease due to defect in primary structure of protein.
20. Name the methods of separation of proteins.
21. What is meant by Edman’s degradation?
22. What is prion disease?
23. What is secondary structre of protein seen in amyloidosis?
24. Comment on sequence of amino acids in collagen.

PROTEIN METABOLISM
Long Questions
1. What are various sources of nitrogen in our body? How nitrogen is disposed from our body?
2. Explain reactions of urea cycle in detail. Write a note on defects associated with urea cycle. Add a
note on regulation of urea cycle.
Short questions
1. Transamination
2. How ammonia is transported in blood?
3. Oxidative deamination
4. What is the significance of glutamine in context of nitrogen disposal?
5. Differentiate between CPS-I and CPS-II
6. What is amino acid pool? Write a note on Nitrogen balance.

INDIVIDUAL AMINO ACID METABOLISM

Long Questions:
1. Explain the major pathway by which phenylalanine gets metabolized. Name three inborn errors that
occur in phenylalanine & tyrosine metabolism. Name the enzyme defect in each of them.
2. Give an account of metabolism of branched chain amino acid. Add a note on abnormalities
associated with their metabolism
3. Name the sulphur containing amino acid. Describe the metabolism of methionine.
4. Explain glycine catabolism and formation of important products derived from glycine.
5. Name the aromatic amino acids. Which of them will give rise to catecholamines. Write the
catecholamine synthetic pathway and its mode of degradation. What is importance of its excretory
products.

Short notes
1. Write a note on enzyme defect & clinical features of Phenylketonuria (PKU).
2. What is the test performed for detecting PKU. What is the dietary advice given to PKU patient.
3. Essential amino acids
4. Name the special products derived from tyrosine metabolism.
5. Outline the steps of creatine biosynthesis.
6. What is active methionine? How it is formed? Give two reactions where it is used.
7. How is gamma amino butyric acid (GABA) formed in the body. Mention its role.
8. Write a note on albinism
9. What are aminoacidurias?
10. Indicate the biochemical defect in Maple syrup urine disease & Hartnup disease
11. Transmethylation
12. Hyperhomocystinaemia & Homocystinuria
13. What is carboxylation and decarboxylation products of glutamic acid. Name the coenzyme involved
in these reaction.
14. What is active sulphate. What are its uses.
15. What is glutathione. Name the amino acids that form glutathione
16. What is serotonin? What is its acetylated and methylated products
17. Name the amino acid which forms vitamin niacin. What is the the neurotransmitter synthesized
from that amino acids?
18. Enumerate Ketogenic amino acids.
19. Name the enzyme deficient in alkaptonuria. How can you detect the presence of homogentisate in
urine.
20. Name the biologically important compound derived from tryptophan
21. Write a note on one carbon metabolism
22. Name the amino acid from which melanin is synthesized

NUCLEOTIDE METABOLISM
General
1. Name the sources of carbonds and nitrogens of purine and pyramiding ring.
Purine Metabolism
1. Name the first committed step in Purine biosynthesis. Mention major steps in purine
biosynthesis. How is denovo pruine biosynthesis regulated?
2. What are salvage pathways in purine metabolism? What is Lesch-Nyhan Syndrome (Focus
on enzyme deficiency, hyperuricemia and self mutilation)?
3. What is the pathway for breakdown of purine nucleotides? What is the end product of
purine catabolism?
4. What is gout? Enumerate various causes of gout with rationale how they cause
hyperuricemia (Focus on overactivity and underactivity of enzymes causing it).
5. Enumerate the clnical findings in gout. What is the mode of action of drug allopurinol in
this condition?
6. Why allopurinol is given to patients with leukemia? Why hyperuricemia is generally seen
in patients with leukemia
7. What is the normal level of uric acid? Write a note on hyperuricemia.

Pyrimidine metabolism
1. How is carbamoyl phosphate formed? Mention major steps in purine biosynthesis.
2. Distinguish between CPS-I & CPS-II
3. How is pyrimidine biosynthesis regulated?
4. Orotic aciduria
5. Mention the end products of pyrimidine catabolism.
Plasma Proteins
1. How are plasma protein separated by electrophoresis. What is the significance of M Band?
2. What are the important functions of albumin? Give major causes and menifestations of
Hypoalbuminemia.
3. Enumerate major transport proteins of plasma and list out their functions.
4. Name the substances that are carried by albumin.
5. Name protein related to emphysema.
6. Draw normal serum electrophoretic pattern and pattern in multiple myeloma, cirrhosis and
nephritic syndrome.
7. What is haptoglobin? Write its importance.
8. What is A:G ratio? How is it helpful in diagnosis?
9. What are Acute phase proteins? Give three examples mentioning their clinical significance.
10. What is meant by salting in and salting out? How it is used for separation of albumin from
globulin?

MOLECULAR BIOLOGY
Structure of DNA
1. Describe the structure of tRNA?
2. Indicate two differences between the nascent mRNA and mature mRNA.
3. What are different eukaryotic RNA polymerases?
4. Which component of nucleotide stores and transmits the genetic information in DNA?
What is the role of sugar and phosphate residues in DNA?
5. Which protein is involved in DNA packing?
6. Role of histones in maintaining DNA intergrity
7. What is frame shift mutation?
8. Mitochondrial DNA

Replication, Repair, Mutation

1. What is semiconservative replication? Explain with a simple diagram.
2. Describe the process of DNA replication with suitable illustration.
3. What is a template strand of DNA?
4. Write on DNA polymerases
5. What are okazaki fragments
6. Explain DNA synthesis on lagging strand of DNA
7. What is the role of topoisomerase and helicase in DNA replication
8. Inhibitors of replication
9. Name the primer required for DNA polymerase III?
10. Write about DNA repair mechanism
11. Role of telomerase in carcinogenesis
12. Explain the term point mutation? Give one example of point mutation
13. What are the different types of DNA repair mechanism?
14. Explain nucleotide excision repair of DNA and mention its importance.
Transcription
1. What is transcription in RNA study?
2. What is transcription unit?
3. TATA box
4. Describe the transcription events in eukaryotes and its regulations.Add a note onpost
transcriptional modification.Discuss about the inhibitors of transcription.(MD)
5. What is post transcriptional modification? Explain with two examples.
6. Vit. C plays a role in post translational modifications. Justify.
Translation
1. What is genetic code? Mention three important features of the genetic code. What are
synonymous codons?
2. Mention three stop codons.
3. What is degeneracy of codons?
4. Write in detail about translation. Add a note on post translational modifications
5. What are post translational modifications? Give two examples.

Regulation of Gene Expression

1. Operon
2. What is regulatory gene?

RDT
1. What are restriction endonucleases? (2)
2. What is gene therapy? Explain. (3)
3. What is probe in relation to nucleic acid analysis? Enumerate the types.
4. What is PCR? What are its applications? (3)
5. Name the enzyme that is used for polymerase chain reaction? It is active upto what
temperature?
6. Name the retrovirus that produces immune deficiency in humans. Which enzyme is
necessary for these viruses to multiply? (2)
7. Reverse transcripitase (3)
8. What is chimeric DNA . What is a cDNA? (3)
9. Indicate the biochemical defect in xeroderma pigmentosa (1)
10. Genetic engineering…
11. What is plasmid DNA? Why is it commonly used for Genetic engineering? (2+2)
12. Write two uses of recombinant DNA. (1)
13. Mention the application of molecular cloning in medicine.(1)
14. What is Chimeric DNA? What is cDNA? (3)
What is the principle of southern blotting. Give two applications. (3)
Describe the applications of recombinant DNA technology (5)
Explain the Western blot technique 10. Describe
the applications of RFLP and PCR. (5)
Principle and applications of recombinant DNA technology (3)