Download CHE-09 Biochemistry

CHE-09
Assignment Booklet
Bachelor’s Degree Programme (B.Sc.)
Biochemistry
Elective Course in Chemistry and
Life Sciences
School of Sciences
Indira Gandhi National Open University
New Delhi, 110068
2007
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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Before attempting the assignments, please read the following instructions carefully.
1
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Assignment No.
Assignment – 1 (TMA)
Assignment – 2 (TMA)
6
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2
Assignment – 01
Tutor Marked Assignment
Biochemistry
Elective Course in Chemistry & Life Sciences
Course Code: CHE-09
Assignment Code :CHE-09/TMA-01/2007
Maximum Marks: 100
Answer all the questions given below.
Q.1 a)
b)
c)
Q.2 a)
b)
Q.3 a)
b)
Q.4 a)
b)
How are the cell organelles isolated and what properties are responsible for their
isolation?
Mention any four differences between prokaryotic and eukaryotic cells.
Explain two important functions of the cell membrane in a cell
What are reducing sugars? How glucose is chemically detected? Give the reactions
involved. Write the structural formula of D-Gluconic acid and D-Galactonic acid.
What are the storage polysaccharides present in animals and plants? Explain the
structural differences between them.
Define essential fatty acids. What do you understand by the following notations used
for two different fatty acid?
i)
18:2, 9, 12
 -3, 6, 9, C18:3
ii)
(5)
(5)
(5)
What are lipoproteins? Discuss their major groups.
(5)
Enlist the different structural forms of DNAs and give the salient features of the Zform.
Write important steps involved in transcription.
(5)
(5)
Q.5 Write short notes on the followings:
a)
DNA denaturation
b)
Golgi bodies
c)
Blood groups
(3+3+4)
Q.6 Answer the following questions in brief.
a)
What are the functional groups attached to  carbon of an amino acid?
b)
Why are the amino acids forming a polypeptide chain called amino acid residues?
c)
What are the characteristics of a peptide bond? List four characteristics.
d)
Which type of amino acids are responsible for acidic or basic properties of a
protein? Give two examples for each.
e)
Which amino acid contributes to the formation of disulphide bonds? What is the
significance of disulphide bridge in protein structure.
Q.7 a)
b)
List and define the weak interactions that contribute to protein structure.
Differentiate between -helix and -pleated sheet structure of proteins.
Q.8 a)
Name the two terms that describe the kinetic behaviour of any enzyme? What do
these signify.
Why is the rate of an enzyme catalysed reaction not a linear function of substrate
concentration?
b)
(4)
(4)
(2)
3
(25)
(6)
(4)
(4)
(3)
c)
Q.9 a)
b)
Q.10 a)
b)
Why do the graphs for pH versus reaction rate and temperature versus reaction rate in
case of enzymatic reactions show a similar behaviour?
(3)
Write down the coenzymes for which the following vitamins function as precursors.
i)
pantothenic acid
ii)
riboflavin
iii) niacin
iv) thiamine
Also give reasons for why dietary deficiencies of the above result in fatigue.
How do competitive and noncompetitive inhibitors alter an enzyme activity?
(6)
Fill in the blank spaces with appropriate words.
i)
……….. metal is a part of vitamin B12.
ii)
Allosterie effectors function by binding to ………………. site on the enzyme.
iii) The class of enzymes responsible for join together two molecules is called
……………
iv) The oxygen binding ability of hemoglobin is due to ………….. group.
v)
Keratins which are responsible for protein structure like, hair, wool, claws
etc. have a ………………………………….. structure.
vi) A tripeptide has ………… peptide bonds and ……… amino acids.
(6)
Explain the following in brief.
i)
Role of iron in electron transport chain
ii)
Role of manganese in water splitting enzymes during photosynthesis
(4)
4
(4)
Assignment – 02
Tutor Marked Assignment
Biochemistry
Elective Course in Chemistry & Life Sciences
Course Code: CHE-09
Assignment Code :CHE-09/TMA-02/2007
Maximum Marks: 100
Answer all the questions given below.
Q.1 Choose the correct statement out of the following given regarding G and describe
why the others are incorrect.
a)
G is directly proportional to G, the standard free energy change for biochemical
reactions.
b)
G is equal to zero when concentrations of reactants and products are no longer
changing.
c)
G can only be calculated when the concentration of reactants and products is
one mole each.
d)
G will indicate the rate and direction of the reaction, if the G and the
concentrations of reactants and products are known.
e)
G is zero when Keq is zero.
Q.2 a)
b)
c)
Q.3 a)
b)
c)
The reaction, fructose - 6-phosphate + Pi
fructose - 1,6-bisphosphate + H2O,
has a Keq of 0.0001 at pH 7. What is the G for this reaction?
Conversion of glyceraldehyde – 3 – phosphate to 1, 3 – bisphosphoglycerate is an
example of substrate level phosphorylation. Explain how?
How is the proton motive force determined during oxidative phosphorylation? What
would happen if the mitochondrial membrane became permeable to protons freely?
In an actively working muscle there is a lot of glycolytic activity. Explain why?
What is the function of the oxygen in electron transport chain?
How does the product of glycolysis enter the citric acid cycle? Does this reaction
generate ATP? If yes, how?
Q.4 Answer the following questions in brief.
a)
How many turns of the TCA cycle are needed to convert acetyl CoA into two
molecules of CO2 and H2O?
b)
How many moles of oxaloacetate are consumed in the TCA cycle for each mole
of CO2 produced?
c)
How does phosphorylase kinase a affect glycogen breakdown?
d)
How many times ATP is used to add to coenzyme A in the oxidation of a
16-carbon fatty acid and with a 18-carbon fatty acid?
e)
What is anaplerosis? How is the availability of pyruvate significant for it?
(10)
(3)
(3)
(4)
(3)
(2)
(5)
(25)
Q.5 a)
b)
c)
How is hexokinase controlled? Of what biological use is this control?
What is the C4 pathway? How is it advantageous over C3 pathway?
How is the dark reaction of photosynthesis different from the glucose metabolism?
(3)
(4)
(3)
Q.6 a)
b)
List various steps of protein biosynthesis. Describe the first two steps in detail.
What are antibiotics? How does streptomycin act as an antibiotic?
(6)
(4)
5
Q.7 a)
b)
Q.8 a)
b)
Q.9 a)
b)
c)
Q.10 a)
b)
c)
What is fermentation biotechnology? How is fermentation method used to produce
penicillin?
What is the immobilization of enzymes and how is this process carried out?
How can somatostatin be produced by Recombinant DNA Technology. Discuss
with illustrations.
Explain the following terms.
(i)
Carcinogens
(ii)
Operon
(6)
(4)
(6)
(4)
Fill in the blank spaces with appropriate words.
(i)
……………. is the carrier of genetic information in all cellular life.
(ii)
Somatic cells of ……………….. had twice the amount of DNA as
compared to corresponding germs cells.
(iii)
DNA is synthesized in the cell from the four ……………………..
(iv)
The enzyme involved in RNA synthesis is called …………………
Name three types of RNAs found in the cell.
Give the full form of the following.
(i)
GTP
(ii)
CTP
(iii)
UTP
(4)
What is difference between immunity and hypersensitivity?
What do you understand by the following?
(i)
Mucoprotein
(ii)
Interferon
(iii)
Pathogens
Discuss the structure of antibodies.
(2)
(3)
6
(3)
(3)
(5)