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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