Download Assignment CHE-09 TMA-01,02 Year 2005

CHE-09
Bachelor’s Degree Programme (B.Sc.)
Spectroscopy
School of Sciences
Indira Gandhi National Open University
New Delhi, 110068
2005-06
1
Dear Student,
We hope, you are familiar with the system of evaluation to be followed for the Bachelor's
Degree Programme. As this stage you may probably like to re-read the section on assignments
in the Programme Guide that we sent you after your enrolment. A weightage of 30 percent, as
you are aware, has been earmarked for continuous evaluation, which would consist of two
tutor-marked assignments for this course. These assignments are provided in this booklet.
Assignment-01 is based on Blocks 1 and 2 whereas Assignment-02 is based on Blocks 3 and 4.
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1.
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Assignment No.
Assignment – 1 (TMA)
Assignment – 2 (TMA)
Submission
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Assignment - 01
Tutor Marked Assignment
Biochemistry
Elective Course in Chemistry and Life Sciences
Course Code : CHE-09
Assignment Code : CHE-09/TMA-01/2005-06
Maximum Marks: 100
Answer all the questions given below.
1.
Discuss the structures and functions of mitochondria and chloroplast in detail.
2.
a) Write equations to show how D-glucose could be converted into:
i) D – Fructose
ii) D – Mannose
iii) Hydroxymethyl furfural
iv) D – Gluconic acid
v) Mixture of formaldehyde and formic acid.
(5)
b) Give the examples of complex polysaccharides and discuss the structure of any
one.
(5)
3.
4.
5.
6.
7.
What is the role of lipids in the formation of biomembrane? Write important functions of
biomembrane.
(10)
(10)
a) Discuss the role of tRNA in protein synthesis.
(5)
b) How is DNA replication carried out in a cell?
(5)
Write short notes on the following.
i) Vacuoles
ii) Mutarotation
iii) Glycogen
iv) Saponification number
v) DNA denaturation
a)
(10)
Write the names and structures of two amino acids each with
i) hydrophobic side chains.
ii) hydrophilic side chains.
iii) chiral side chains.
(6)
b)
Define geometrical isomerism. Explain the existence of this isomerism in a peptide bond. (4)
a)
Where do you find φ and  angles in protein structure? Describe the structure.
(4)
b)
Give two advantages of having a quaternary structure of proteins.
(2)
c)
Describe the function of haemoglobin as a transport protein.
(4)
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8.
a)
How does a coenzyme differ from a prosthetic group? Give an example of a
holoenzyme and its coenzyme.
(3)
Differentiate between the ‘lock and key’ hypothesis and ‘induced fit theory’ of enzyme
specificity.
(4)
What is the significance of proximity and orientation effect in explaining the
specificity of enzymic action?
(3)
a)
State the physiological roles of calcium and iodine.
(4)
b)
Write the components of coenzyme A and folic acid.
(3)
c)
How are isoenzymes different from other enzymes? Give an example of an enzyme
with isoenzyme properties.
(3)
b)
c)
9.
10.
Fill in the blanks with appropriate answers:
i)
Pernicious anaemia results due to the lack of trace element _________ which is a part of
vitamin ________.
ii) The visual process in human beings during night involves a conjugated protein called
__________.
iii) The active coenzymic form of thiamine is called _______________________ which
participates in the ________________ reaction.
iv) The competitive inhibitors are also known as _____________.
v) In lock and key model of enzyme action, the part of enzyme that recognises substrate is
called the _______________.
vi) In the tripeptide Cys – Ser – Leu, the amino acid with free amino end is ____.
vii) Degradation of D-fructose – 1, 6 – bisphosphate to D – glyceraldehyde – 3 – phosphate is
catalysed by a class of enzymes called _________.
viii) The nonextensible property of a silk fibre is due to its _____________ structure.
(10)
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Assignment – 02
Tutor Marked Assignment
Biochemistry
Elective Course in Chemistry and Life Sciences
Course Code : CHE-09
Assignment Code : CHE - 09/TMA-02/2005-06
Maximum Marks : 100
Answer all the questions given below.
1.
a)
b)
What is meant by a spontaneous reaction? How does coupling in biochemical
reactions help these proceed in forward direction?
' values at 298 K. Take the help of
For the following reaction calculate G°΄ and K eq
Table 8.3 given in Unit 8.
3 – Diphosphoglycerate.
(3)
Why is the hydrolytic reaction, ATP
ADP a better choice for most of the
biochemical reactions as compared to ATP
AMP, although the amount of free
energy released in the two cases is almost similar?
(3)
a)
What will happen if NAD+ is not present in the conversion of G-3-P into pyruvate?
(3)
b)
Can sucrose be adsorbed as such by human intestine? State the process of its
absorption.
(4)
How is the step of conversion of pyruvate to phosphoenolpyruvate accomplished
thermodynamically? Write the reaction.
(3)
Explain the phenomenon of substrate channelling with an example of pyruvate
dehydrogenase complex involved in the conversion of pyruvate to acetyl-CoA.
(5)
How is the isotopic tracer technique helpful in predicting the stereochemistry
of TCA cycle?
(5)
What is the mechanism of regulation of glycolysis? Explain with the help
of an example.
(4)
What is effect of high ATP/ADP or NADH/ NAD+ ratios on the rate of TCA cycle?
Explain briefly.
(3)
Describe the energetics of a fat metabolism in general.
(3)
3-Phosphoglycerate
c)
2.
c)
3.
a)
b)
4.
a)
b)
c)
5.
(4)
1,
Describe the following terms in brief.
a)
b)
c)
d)
e)
Red drop
Photophosphorylation
Fluorescence
Funnelling effect
Hill reaction
(2  5)
5
6.
7.
8.
9.
10.
a)
Discuss the role of initiation and termination codons in protein synthesis.
(6)
b)
How are amino acids activated for polypeptide synthesis? Explain.
(4)
a)
How is somatostatin produced by recombinant DNA technology? Draw figure to
illustrate the steps.
(6)
b)
What is an immobilised enzyme? How is enzyme immobilisation process carried out?
(4)
a)
Discuss the role of following in protein biosynthesis:
i) A and P sites
ii) Repressor
(5)
b)
Discuss the preparation of vinegar from sugar containing material.
(5)
a)
i) DNA was isolated from nuclei of the ______________.
ii) Virus which attack bacteria are called ______________.
iii) An important enzyme involved in DNA replication is ____________.
(3)
b)
How many types of RNAs are present in a cell? Give their names.
(3)
c)
Write the full form of the following
i) d-ATP
ii) d-GTP
iii) d-CTP
Give structure of any one of them.
(4)
Explain the following term in one or two lines.
i) Antigen
ii) B-cells
iii) Antitoxin
(3)
Fill in the following blanks
i) The antibody molecules consist of four ___________ chain.
ii) Chemotactic factor draws ___________ to antigen site.
iii) Stem cells arise in ____________.
(3)
Discuss antigen- antibody interaction briefly.
(4)
a)
b)
c)
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