LOYOLA COLLEGE (AUTONOMOUS), CHENNAI –600 034

B.Sc., DEGREE EXAMINATION – CHEMISTRY

FIFTH SEMESTER – NOVEMBER 2003

CH – 5401/520/CHE 401 – BIO-CHEMISTRY

10-11-2003                                                                                                     Max:100 marks

1.00 – 4.00

PART – A

Answer ALL the questions.                                                                              (10×2=20 marks)

1. Define isoelectric point.
2. How is aninoacid tested using Ninhydrin? Indicate the reaction.
3. What are the two tertiary structures possible for a polypeptide? Give one example for each.
4. What is transamination reaction? Mention one example.
5. What is ATP? Give its structure.
6. What is ‘allosteric’ enzymes? How does it affect the rate of a reaction?
7. Suggest a chemical test for cholesterol.
8. What is the reaction of glucose with an amine?
9. Indicate the hydrogen bonding between A – T, G-C.
10. Mention any two differences between DNA and RNA?

 

PART – B

Answer any EIGHT questions.                                                                        (8×5=40 marks)

11. Suggest a synthetic route for ala-gly-ph ala.
12. Explain one method for C-terminal analysis of a polypeptide?
13. Explain all the steps involved in the ‘b-oxidation of fattyacid’.
14. How is the ring size of glucose determined?
15. Write briefly about competitive inhibition of enzymes.
16. How are enzymes classified? How is the enzyme action affected by pH?
17. Explain the mechanism of oxidative phosphorylation and explain the steps involved in this process.
18. Bring out the salient features of secondary structure of DNA.
19. Define genetic code. How is genetic information decoded for protein synthesis?
20. Write all the steps involved in the bio-synthesis of fattyacids.
21. Explain how blood is coagulated?

 

PART – C

Answer any FOUR questions.                                                                         (4×10=40 marks)

22. a) Define anabolism and catabolism. How are amino acids catabolyzed?
23. b) Discuss the advantage of preparing polypeptides by solid phase synthesis.
24. Explain how Michalis-Menton model helps in understanding the characteristics of enzyme catalysis. Derive the expression for the rate of enzyme catalysis.
25. Out line the steps in the bio-synthesis of cholesterol.
26. Describe the secondary structure of proteins.
27. Describe the steps involved in a) tricarboxylic acid cycle b) Glycolysis and energetics of glycolysis.
28. Explain the mechanism of transport of oxygen by blood.

 

 

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                          LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – CHEMISTRY

AD 08

FIFTH SEMESTER – NOV 2006

CH 5401 – BIO CHEMISTRY

(Also equivalent to CHE 401/CH 520)

 

 

Date & Time : 01-11-2006/9.00-12.00   Dept. No.                                                       Max. : 100 Marks

 

 

 

PART – A

Answer all the questions                                                     (10 ×2 = 20 marks)

 

1. What are essential amino acids? Give any two examples.
2. Define point mutation. Explain with respect to sickle cell anaemia.
3. Mention the factors influencing enzyme action.
4. What are waxes? Give example.
5. Expand the terms EFA and PUFA. Give an example for each.
6. Draw the pyranose structure of glucose and the furanose structure of fructose.
7. ‘Glycogen highly branched whereas starch is not.’ Why?
8. Explain the fork model for DNA replication.
9. What are plasma proteins? Give example.
10. Define the terms catabolism and anabolism.

 

 

 

PART – B

Answer any eight questions                                                (8 × 5 = 40 marks)

 

11. Give the structure and functions of the following organelles.
    a) centriole b) lysosome                 c) chloroplast.
12. How are proteins sequenced from the N-terminal using Edmann’s reagent and C- terminal using enzymes?
13. Define enzyme immobilization. Explain the various methods of enzyme immobilization.
14. Give the advantage of solid-phase peptide synthesis. Explain how peptides are synthesized by solid phase method.
15. What are coenzymes? Explain the mechanism of coenzyme action.
16. Explain the biosynthesis of cholesterol.
17. Define the following with suitable examples
    a) Hydrogenation of fats.
    b) auto-oxidation of fats
    c) saturated and unsaturated fatty acids.
18. ‘Starch is edible whereas cellulose is not.’ Explain.
19. Explain glycolysis.
20. Differentiate between DNA and RNA.
21. Explain the electron transport chain.
22. How is blood coagulated?

 

 

 

 

 

 

 

 

 

 

 

PART – C

Answer any four questions                                                (4 × 10 = 40 marks)

 

23. Explain the following
    a) Strecker’s synthesis of amino acids
    b) Phthalimide synthesis of amino acids
    c) Reaction of ninhydrin with amino acids
    d) ornithine cycle
24. What are inhibitors? Explain competitive, non-competitive and allosteric inhibitions.
25. a) How are fatty acids biosynthesized?
    b) How are triglycerides biosynthesized?
26. a) Explain TCA cycle.
    b) Define mutarotation and explain with reference to glucose.
27. How are proteins biosynthesized?
28. Explain the following
    a) DNA replication.
    b) The base pairing in DNA
    c) DNA is the genetic material whereas RNA is not.

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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc.

LM 16

DEGREE EXAMINATION –CHEMISTRY

FIFTH SEMESTER – APRIL 2007

CH 5401 – BIO CHEMISTRY

 

 

Date & Time: 02/05/2007 / 1:00 – 4:00          Dept. No.                                                     Max. : 100 Marks

 

 

PART – A

Answer all the questions                                                     (10 ×2 = 20 marks)

1. Define isoelectric point of an amino acid.
2. Mention the components of the nucleus and give their functions.
3. Define enzyme immobilization.
4. What happens during rancidification?
5. How is starch different from glycogen?
6. What are sterols? Give an example.
7. What is Sanger’s reagent? Mention its use.
8. What are plasma proteins? Give an example.
9. What are carbohydrates? How are they classified?
10. Why DNA is the genetic material whereas RNA is not?

 

                                                           PART – B

Answer any eight questions                                                (8 × 5 = 40 marks)

11. a) What is meant by denaturation of proteins?
    b) Give the mechanism of reaction of amino acids with ninhydrin.
12. Explain the structure and functions of the following organelles
    a) cell wall b) golgi apparatus                    c) vacuole
13. Suggest a method of synthesis for the following amino acids
    a) alanine b)methionine                           c) cysteine.
14. Explain the mechanism of enzyme catalyzed reaction using Lock and Key and Induced fit models.
15. How are fats classified? Give suitable examples.
16. Explain β-oxidation of fatty acids.
17. Elucidate TCA cycle.
18. Write note on the electron transport chain.
19. Name the different types of RNA and list down their functions.
20. ‘DNA replicates semi-conservatively’. Explain.
21. What is a genetic code? Give its significance.
22. How are phospholipids classified? Give suitable examples.

 

PART – C

Answer any four questions                                                (4 × 10 = 40 marks)

23. Explain the following
    a) deamination b) transdeamination
    c) transamination         d) ornithine cycle
24. What are inhibitors? Explain competitive, non-competitive and allosteric inhibitions.
25. a) How are fatty acids biosynthesized
    b) What are phospholipids? How are they classified?
26. Explain glycolysis.
27. a) Distinguish between animal and vegetable fats.
    b) Give the various steps involved in oxidative phosphorylation.
28. How are proteins biosynthesized?

 

 

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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – CHEMISTRY

GH 17

FIFTH SEMESTER – APRIL 2008

CH 5401 – BIO CHEMISTRY

 

 

 

Date : 06/05/2008                Dept. No.                                        Max. : 100 Marks

Time : 1:00 – 4:00

            PART A

Answer all the questions                                                                                                         10 x 2 = 20

1. What are the functions of nucleus?
2. What is Zwitter ion?
3. What are ligases? Give an example.
4. Draw the structure of cholesterol.
5. What are the products obtained by the oxidation of fructose?
6. What are the differences between cellulose and starch?
7. Write a note on biological oxidation?
8. What is the role of ubiquinone in electron transport mechanism?
9. What are purine and pyrimidine bases?
10. Write down the various types of RNA.

PART B

Answer any eight questions                                                                                        8 x 5 = 40

11. Explain the primary structure of proteins.
12. How is N-terminal of an amino acid determined by Sanger’s method?
13. How is alanyl glycine prepared?
14. Explain the factors affecting the enzyme activity.
15. Discuss β-Oxidation of fatty acids.
16. Discuss any three important phospholipids.
17. Explain the cyclic structure of D-glucose.
18. Explain the classification of carbohydrates with examples.
19. Discuss the mechanism of oxidative phosphorylation.
20. Draw the structure of hemoglobin. Write any two the functions of hemoglobin.
21. Explain the clover leaf model of t-RNA.

22     Discuss the replication of DNA.

PART C

Answer any four questions                                                                               4 x 10 = 40

23. a) Explain the secondary structure of proteins.
24. b) Describe any two methods of preparation of amino acids.
25. a) Explain the steps involved in absorption and digestion of proteins.
26. b) What are the differences between animal and plant fats?
27. Describe different types of enzyme inhibition.
28. Explain the overall process of glycolysis with enzymes involved in each step and energy yield.
29. Explain the role of RNA involved in protein biosynthesis.
30. Explain the double helical structure of DNA.

 

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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – CHEMISTRY

DB 16

FIFTH SEMESTER – November 2008

CH 5404/CH 5401 – BIO CHEMISTRY

 

 

 

Date : 14-11-08                     Dept. No.                                        Max. : 100 Marks

Time : 9:00 – 12:00

PART A

Answer ALL the questions.                                                                                                             (10 x 2 = 20)

 

1. What are the functions of cytoplasm of the cell?
2. How is the presence of aldehyde group confirmed in glucose?
3. What are essential fatty acids? Give an example.
4. Define iodine number of an oil.
5. Write down the differences between amylose and glycogen.
6. What is glycosidic bond? Give an example.
7. What is respiration? What are the two phases of respiration?
8. Define oxidative phosphorylation.
9. Draw the structure of adenylic acid.
10. What are coenzymes?

PART B

Answer any EIGHT questions.                                                                                                        (8 x 5 = 40)

 

11. Write down the differences between Prokaryotic and Eukaryotic cells.
12. Discuss the β-Oxidation theory of fatty acids.
13. What are phospholipids? Explain the types of phospholipids.
14. Mention any five differences between animal and plant fats.
15. Discuss any five characteristic features of biological oxidation.
16. Explain the classification of carbohydrates with examples.
17. Discuss briefly the phase II of the glycolysis process.
18. Discuss the mechanism of electron transport system.
19. Explain the replication of DNA.
20. Draw and explain the double helical structure of DNA.
21. Explain the steps involved in the translation process of protein synthesis.
22. How is the cyclic structure of glucose elucidated?

 

PART C

Answer any FOUR questions.                                                                                                         (4 x 10 = 40)

 

23. Discuss any two methods to determine the N-terminal of an amino acid.
24. Explain the types of reversible enzyme inhibition.
25. Explain the series of reactions involved in TCA cycle with the enzymes involved and energy yield.
26. Discuss the biosynthesis of cholesterol.
27. a) Draw and explain the structure of t-RNA.
28. b) Explain the importance of primary structure of proteins.                                                                   (5+5)
29. a) Explain the chemistry of hemoglobin in blood.
30.  b) What is genetic code? Mention any five important characteristics of genetic                           (5+5)

 

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   LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – CHEMISTRY

WD 16

FIFTH SEMESTER – April 2009

CH 5404 / CH 5401 – BIO CHEMISTRY

 

 

 

Date & Time: 30/04/2009 / 1:00 – 4:00       Dept. No.                                                       Max. : 100 Marks

 

 

PART A

Answer all the questions.                                                                                   10 x 2 = 20

1. Give any two functions of the nucleus.
2. How is glycine prepared by Strecker synthesis?
3. Define catabolism.
4. How is C-terminal of an amino acid determined?
5. What are coenzymes?
6. Define iodine number of an oil.
7. What will happen when glucose and fructose are oxidized by conc. HNO₃?
8. Draw the structure of purine and pyrimidine bases in DNA.
9. Define oxidative phosphorylation.
10. Mention any two differences between amylose and amylopectin.

PART B

Answer any eight questions.                                                                                8 x 5 = 40

11. How is N-terminal of an amino acid determined by Sanger’s method?
12. Describe the synthesis of glycyl alanine by t-BOC method?
13. Explain the biosynthesis of fatty acids.
14. Discuss the b-oxidation theory of fatty acids.
15. Mention differences between prokaryotic and eukaryotic cells.
16. What are phosopholipids? How are they classified? Explain.
17. Discuss the mechanism of electron transport reaction.
18. Draw and explain the structure of t-RNA.
19. Briefly explain the replication of DNA.
20. What is genetic code? Mention any four important characteristics of the genetic code?
21. Describe the role of hemoglobin in the chemistry of respiration.
22. What are the factors affecting the enzymatic activity?

PART C

Answer any four questions.                                                                              4 x 10 = 40

23. What are the different chemical bonds involved in protein structure? Explain.
24. Define enzyme inhibition. Explain the types of inhibition with examples.
25. a) Define biological oxidation. Give any five salient features of biological oxidation.
26. b) Mention any five differences between plant and animal fats. (5+5)
27. How is glucose converted to pyruvate? Explain.
28. Draw and explain the citric acid cycle with all the steps involved.
29. Discuss the biosynthesis of proteins in brief.

 

 

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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – CHEMISTRY

FIFTH SEMESTER – APRIL 2012

CH 5404 – BIO CHEMISTRY

 

 

Date : 30-04-2012              Dept. No.                                        Max. : 100 Marks

Time : 1:00 – 4:00

 

Part A

Answer ALL questions.                                                                                      (10 x 2 = 20 Marks)

 

1. What is a peptide bond?
2. Define denaturation of a protein.
3. Give an example for the geometric specificity of an enzyme.
4. Mention the significance of enzymes in the kinetics of the reaction.
5. Define RM value of a fat.
6. Draw the structure of cholesterol.
7. Mention the differences between amylose and amylopectin.
8. What are disaccharides? Give an example.
9. Mention any two differences between DNA and RNA.
10. Define genetic code.

 

Part B

Answer any EIGHT questions                                                                             (8 x 5 = 40 Marks)

 

11. How is Sanger’s method useful for the determination of amino acid sequence?
12. Mention the differences between plant and animal fats.
13. Briefly discuss the primary structure of proteins.
14. What are the factors affecting the enzyme activity? Explain.
15. What are phospholipids? Explain the types of phospholipids.
16. Explain the mechanism of electron transport chain.
17. What is payoff phase? Explain the steps involved.
18. Discuss briefly the translation process.
19. Mention any five salient features of biological oxidation.
20. Draw and explain the replication of DNA.
21. Define rancidity? Explain the types of rancidity.
22. Draw and explain the structure of t-RNA.

 

Part C

Answer any FOUR questions                                                                           (4 x 10 = 40 Marks)

 

23. Explain the secondary structure of proteins.
24. What is enzyme inhibition? Explain any two types of enzyme inhibition.
25. ) Discuss the β-oxidation theory of fatty acids.

b.) Explain the coenzyme action in brief.                                           (5 + 5)

26. Draw and explain the steps involved in TCA cycle.
27. Explain in detail the characteristics of enzymes.
28. Draw and explain the double helical structure of DNA.

 

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