LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

             B.Sc. DEGREE EXAMINATION – PLA. BIO&BIOTEC.&ADV.ZOO.&BIOTE.

GH 14

FOURTH SEMESTER – APRIL 2008

CH 4204 / 4202 – CHEMISTRY FOR BIOLOGISTS – II

 

 

 

Date : 24/04/2008                Dept. No.                                        Max. : 100 Marks

Time : 9:00 – 12:00

 

PART – A

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

1. What is feed back inhibition ? Give an example.
2. Define iodine value of oil.
3. Give any two differences between DNA and RNA.
4. How will you prepare BHC ?
5. Explain about vanslyke method.
6. What is apoenzyme ?
7. Draw the structure of flavones.
8. How will you prepare glucaric acid from glucose ?
9. Give the structure of the following. i) Citral ii) a- Pinene
10. What is absolute specificity ?

 

PART – B

Answer any EIGHT questions only.                                                   (8 X 5 = 40)

 

11. How will you form Gly-Ala peptide bond by Fisher’s third method ?
12. Explain about Lobryde Bruyn Van Elestein rearrangement.
13. Give the difference between plant and animal fatty acids.
14. Explain about hydrogen bonding between the nitrogenous bases in DNA.
15. How will you analyse C- terminal of aminoacid by enzymatic method ?
16. What is an alkaloid ? Give it’s classification.
17. Write short notes on superphosphate.
18. Show that D- glucose and D- fructose form the same osazone.
19. What are the steps involved in citric acid cycle ? Calculate the net ATP’s gained.
20. How did Haworth establish the presence of six membered ring in glucose.
21. What are the factors which affect the activity of the enzyme ? Explain any two.
22. Write short notes on rancidity.

 

 

 

PART – C

Answer any FOUR questions only.                                      (4 X 10 = 40)

 

23. How will you convert the following :-
24. a) Aldohexose into aldopentose (6)
25. b) Aldopentose into aldohexose.                       (4)
26. Give the role of macro nutrients and explain each with examples.
27. Explain the mechanism of enzyme action.
28. What are fungicides ? Explain it with two examples.
29. Derive Michelis- Menton equation and explain each terms involved.
30. Discuss the following :-
31. a) Manufacture of Urea                                                                        (6)
32.  b) Three types of RNA                                                                         (4)

 

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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

             B.Sc. DEGREE EXAMINATION – PL.BIO.&BIOTEC.&ADV.ZOO&BIOTECH.

GH 8

THIRD SEMESTER – APRIL 2008

CH 3104/ 3102 – CHEMISTRY FOR BIOLOGIST – I

 

 

 

Date : 07-05-08                  Dept. No.                                        Max. : 100 Marks

Time : 9:00 – 12:00

 

PART-A

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

 

1. Predict the hybridization and shape of the following molecules.

(a) BF₃            (b) PCl₅

2. Draw the structure of the following complexes.

(a) tetraamminecopper(II) sulphate   (b) Potassium hexacyanoferrate(III)

3. Calculate the normality of a solution having 9.8g of H₂SO₄ in 2 litre water.                (Equivalent weight of H₂SO₄ = 49)
4. Define pH of a solution .What is the pH of pure water
5. Differentiate order and molecularity of a reaction.
6. Synthesis of ammonia is a heterogeneous catalysis reaction. Justify.
7. Mention the optical properties of colloids.
8. What is meant by coagulation? Give an example.
9. How will you synthesise Terylene? Mention its use.
10. Why tertiary carbonation is more stable than secondary and primary? Give reasons.

 

PART-B

 

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

 

11. Write a note on vander Waals forces.
12. Explain the structure and function of hemoglobin.
13. Discuss the structure of methane based on hybridization.
14. (a) State the law of volumetric analysis.                                                           (2)

(b) 20ml of oxalic acid requires 19.8 ml of 0.095N of NaOH. Calculate the weight

of crystalline oxalic acid present in 500ml of the given solution.                    (3)

15. What is a buffer solution? Discuss the buffer action of a mixture of ammonium hydroxide hydroxide and ammonium chloride.
16. Derive the rate expression for the rate constant of a first order reaction.
17. (a) Define t_1/2 of a second order reaction.                                                          (3)

(b) What is a zero order reaction? Give an example.                                         (2)

18. Write a note on electro osmosis.
19. (a) How will you prepare ferric hydroxide sol by peptisation method?            (3)

(b) Write any two applications of colloids.                                                        (2)

20. Define inductive effect. Mention its types with examples.
21. What are polymers? Explain the classification of high polymers giving one example of each.
22. Discuss the optical activity in lactic acid.

 

PART-C

 

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

 

23. (a) Explain Werner’s theory of coordination complexes.            (6)

(b) Draw all possible isomers of  [Rh(en)₂Br₂]⁺ complex.                                  (4)

24. (a) Discuss the types of hydrogen bonding with suitable examples.            (6)

(b) Discuss the structure of NaCl unit cell.                                                        (4)

25. (a) What are primary and secondary standard solutions.           (4)

(b) What is common ion effect? Give an example.                                            (3)

(c) Is NaOH a primary standard? Explain your answer.                                    (3)

26. Discuss the kinetics of enzyme catalysed reaction.
27. (a) Define the following:

[1] Enantiomers  [2] Diastereomers  [3] Resolution of racemic mixtures    (2+2+2)

(b) Explain the isomerism exhibited by maleic and fumaric acids.                    (4)

28. (a) What are the defects of crude natural rubber? Explain with equation how are they overcome? (6) (b) Discuss any two method of expressing the concentration of a solution.           (4)

 

                        

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       LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

B.Sc. DEGREE EXAMINATION – ADV.ZOO. & PLAN. BIO&BIOTECH.

WD 07

THIRD SEMESTER – April 2009

CH 3104 / 3102 – CHEMISTRY FOR BIOLOGIST – I

 

 

 

Date & Time: 17/04/2009 / 1:00 – 4:00    Dept. No.                                         Max. : 100 Marks

 

 

PART A

Answer all the questions.                                                                                      10×2=20

1. Define molarity.
2. How are (i) ionic and (ii) covalent bonds formed?
3. What is tyndall effect?
4. How is Nylon-6 prepared?
5. Differentiate lyophilic and lyophobic colloids.
6. What is enzyme catalysis?
7. Give the principle of volumetric analysis.
8. What are enantiomers? Give an example.
9. Mention the properties of a primary standard substance.
10. What is electron affinity? What is its significance?

PART B

Answer any eight questions.                                                                                  8×5=40

11. How are         a) PVC       b) Teflon prepared?
12. Explain the following with example
13. a) Inductive effect        b) Resonance effect.
14. Explain the structure and functions of hemoglobin.
15. Explain geometrical isomerism of square planar co- ordination complex.
16. Discuss the postulates of VSEPR theory.
17. Give any two methods of the separation of racemic mixture.
18. Explain the properties of primary and secondary valencies of a coordination

compound

18. a) How will you prepare 250mL of 0.05N NaOH solution (molecular weight-40)
19. b) What is the amount of H₂SO₄ required (in grams) to prepare 500mL of

N/10 H₂SO₄ (molecular weight –98)

19. What are the properties of ionic and covalent compounds?
20. Write short notes on a) peptisation       b) polymerisation.
21. Derive an expression for the half life period for first order reaction from its rate

Expression.

22. a) Arrange the following in the increasing order of strength of acid giving reasons:

(i) CH₃COOH      (ii) CCl₃COOH       (iii) CF₃COOH       (iv) HCOOH

1. b) Arrange the following in the increasing order of strength of the base giving

reasons:

(i) NH_{3                      (}ii) CH₃NH₂           (iii) (CH₃)₂NH         (iv) (CH₃)₃N

 

                                                                                             PART C

Answer any four questions.                                                                                 4X10=40

23. Draw and explain the crystal structures of NaCl and CsCl.
24. a) Write short notes on Dissociation constant of acids.
25. b) What is buffer solution? Derive Henderson equation for acidic buffer.
26. Derive the rate constant for the second order reaction involving same initial concentration of the reactant.
27. Discuss any three methods of preparation of colloids.
28. Explain the hybridization in NH₃, H₂O and BeCl₂ and predict the geometry of these molecules.
29. a) Explain the intermolecular and intramolecular hydrogen bonding.
30. b) Discuss the application of colloids.

 

 

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     LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

WD 13

B.Sc. DEGREE EXAMINATION – PLANT.BIO&BIOTEC.& ADV.ZOO.&BIO.TECH.

FOURTH SEMESTER – April 2009

CH 4204 / CH 4202 – CHEMISTRY FOR BIOLOGISTS – II

 

 

 

Date & Time: 27/04/2009 / 9:00 – 12:00  Dept. No.                                                   Max. : 100 Marks

 

 

PART A

Answer all the questions.                                                                                   10 x 2 = 20

1. Who is called as the father of modern enzymology? Why?
2. Define isoelectric point.
3. How is glycine prepared by strecker synthesis?
4. What are coenzymes?
5. Define rancidity of an oil.
6. Draw the structure of adenine and guanine.
7. How is the presence of ketone group in C-2 position confirmed in fructose?
8. Draw the structures of a) papavarine and b) camphor.
9. Define saponification value of an oil.
10. How is urea prepared?

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. What are the factors affecting the enzymatic activity?
13. What are phospholipids? Explain any two types of phospholipids.
14. Describe the steps involved in the preparatory phase of glycolysis.
15. What are macro and micronutrients? Discuss with examples.
16. Explain the classification of alkaloids.
17. How are the following prepared?
18. a) Superphosphate of lime                     b) DDT                        c) BHC
19. Distinguish glucose and fructose by oxidation and reduction reactions.
20. Explain the isolation of terpenes.
21. Discuss the different types of soil.
22. Describe the importance of flavones and flavanoids.
23. Give any two methods of preparation of an amino acid.

PART C

Answer any four questions.                                                                              4 x 10 = 40

23. What is enzyme inhibition? Explain the types of inhibition with examples.
24. a) Explain the double helical structure of DNA.
25. b) Briefly describe the replication of DNA.        (5+5)
26. Discuss the various steps involved in TCA cycle with the energy yield.
27. How is the structure of glucose elucidated?
28. a) What are coenzymes? Explain the mechanism of coenzyme reaction.
29. b) What is translation? Explain the process in brief.                     (5+5)
30. Explain the primary and secondary structure of proteins.

 

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