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NORTH MAHARASHTRA UNIVERSITY, JALGAON

QUESTION BANK FOR S.Y.BSc. - BIOTECHNOLOGY


PAPER BT 211 & 212 CELL BIOLOGY AND BASIC METABOLISM

SEMESTER- FIRST

(WITH EFFECT FROM JUNE, 2008)

NORTH MAHARASHTRA UNIVERSITY, JALGAON


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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

QUESTION BANK OF BIOTECHNOLOGY

CLASS- S.Y.B.Sc SEMESTER-I


PAPER: BT 211- CELL BIOLOGY AND BASIC METABOLISUM

Unit I: Cell Division & Cell Ageing


Q.1 Question for 2 Marks (Objective). 1). --------- divide cell cycle into four phases a) c) 2). a) c). 3) a) c) 4). a) c) 5). a) c) 6) a) c) 7) a) c) 8) a) c) Darnell Hapler Meosis Median RNA m RNA G1 Phase S phase RNA synthesis Division of cell RNA synthesis Protein synthesis Somatic cell Both a and b Prophase Anaphase b) d) b) d) b) d) b) d) b) d) b) d) b) d) b) d) Bottino Howard Mitotic Post Median r RNA t RNA G2 phase All the above. DNA replication. None of these. DNA replication. none of these. Germ cell. None of these. Metaphase Telophase

M phase of cell cycle is also called ----------

During G2 phase synthesis of ------- continuous

Interphase of cell division includes following phases-----------.

G1 phase of Cell cycle involved --------------.

S phase is carried out by-------------.

Mitotic cell division occurred in------------.

Condensation of chromosome is carried in-------------.

9) Equatorial plate formation is a result of------------.

N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

a) c) 10) a) c) 11) a) c) 12) a) c) 13) a) c)

Prophase Anaphase Pachytene Zygotene Apoptosis Cell lysis Mitosis Interphase

b) d) b) d) b) d) b) d)

Metaphase Telophase. Leptotene Diplotene. Cell ageing. None of these. Meiosis None of these. b) Crossing over d) Tetrad formation

Crossing over is observed in-------------.

Programmed cell death is called as------------.

Chiasmata formation takes place in------------.

Zygotene is characterized by--------------. Chiasmata formation Pairing of homologous chromosomes

Question for 2 Marks (Short Answer) 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) 14) 15) Define: a) Cell cycle b) M phase c) G2 phase Explain cell cycle with definition. Explain interphase. Define meiosis and classify it. Describe Pachytene phase. Explain significance of meiosis. Define apoptosis. Define Meiosis. Define Ageing of cell. Define-Mitotic spindle. Comment on morphological changes in apoptosis. Describe chiasmata formation. Explain cytokinesis. Define and explain apoptosis. Draw cell cycle and explain it briefly.

Question for 3 Marks 2


N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

1) 2) 3)
4) 5) 6) 7)

What is concept of cell Apoptosis?


Give the significance of mitosis.

Comment on sub- cellular mechanism of ageing.


Comment on prophase II and metaphase II. Write a note on telophase and cytokinesis. Discuss about free radical theory of cell ageing. Discuss briefly cell apoptosis.

Question for 4 Marks 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) Comment on Interphase in Cell Division. Describe anaphase of mitosis. Describe meiotic division II. What is Apoptosis? Give its importance. Describe briefly, cell ageing. Comment on metaphase. Comment on prophase. Describe G1 Phase and S phase What is cell cycle? Explain briefly the stages of cell cycle Enlist the stages of cell cycle? Comment on longest stage of Cell Cycle? What basic activities occurring during mitosis? Compare: Mitosis & Meiosis. Compare the cytogenic view & chromatin in interphase in Mitosis & Meiosis.

Question for 6 Marks 1) 2) 3) 4) Explain mitosis in detail. Describe meiotic division I along with diagramme. Enlist the differences between meiosis and mitosis. Describe theories of cell ageing.

5) 6) 7)

Comment on somatic mutation theory. Comment on free radical theory. Comparison & Significant of mitosis & meiosis.
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8)

What is cell division? Discuss the use & biological significance of each type of cell division.

Unit II: Cell Membrane and Transport


Q.1 Question for 2 Marks (Objective). 1) -----------provides rigidity to cell membrane. a) c) 2) a) c) 3) a) c) 4) a) c) 5) a) c) 6) Glycerol Phospholipids b) d) Sterol All the above Cell wall Ribosome Cephalin Sphingomyelin Endocytosis Phagocytosis. Endocytosis Phagocytosis.

Transport is a main function of--------------. Plasma membrane b) Golgi complex Lecithin Glycerol Exocytosis Pinocytosis Exocytosis Pinocytosis d) b) d) b) d) b) d)

-----------type of lipid present in plasma membrane.

Molecules get transported out is called as------------.

Solid particles engulfed by plasma membrane are called as----------.

----------enhances stability of lipid bilayer and reduces their permeability. a) c) Cholesterol Glycerol Exocytosis Pinocytosis Active transport Both a & b b) d) b) d) b) d) Cephalin Sphingomyelin. Endocytosis Receptor mediated Endocytosis. Passive transport. Antiport.

7)

Clathrin formation takes place in------------. a) c) a) c)

8) ------------transport required metabolic energy for its transport.

9)

Na-K ATPase pump is example of----------------type of transport. 4


N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

a) c) 10) a) c) 11) a) c) 12) a) c) 13) a) c) 14) a) c)

Active transport Symport Active transport Symport Lipoprotein Jelly membrane 30% &20% 10% &5% Lipid Protein Lewis Edward b) d) b) d)

b) d) b) d) b)

Passive transport. Antiport. Passive transport. Antiport. Plasma lemma

Chloride shift is example of-------------type of transport.

All cell are bounded by a thin membrane ---------. d) cell membrane b) d) 40%&20% 60% & 40%.

Membrane contain about -------- protein------carbohydrate dry weight.

--------- substance passed easily through cell membrane. Fat soluble Amino acid. Alberts Rothman

The Pinocytosis was first observe by---------in amoeba.

Question for 2 Marks (Short Answer) 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) 14) Comment on distribution of lipid. Describe structure of cell membrane. Explain the mechanism of Exocytosis. Describe the structure of flagella with Diagramme. Comment on Danielli-Davson model. Describe briefly Phagocytosis. Explain Na-K pump. Comment on membrane models. What is active transport? What is passive transport? Describe role of flagella. Explain simple diffusion. Define active and passive transport. Enlist different lipid present in membrane.

N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

15) 16) 17) 18)

Comment on cilia. Comment on transport system of glucose. Describe Phagocytosis briefly. Role of micro filament.

Question for 3 Marks. 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) Explain Cytoskeltal element with help of microtubles. Comment on active transport membrane. What is membrane lipid? Structure of cell membrane. Describe organization of cell membrane. Comment on receptor mediated Endocytosis. Give Antigenic structure account of membrane lipid. Explain passive transport briefly. Describe the structure of lipid bilayer. Organization of cell membrane. Comment on Danielle model. Give the difference between Phagocytosis and Pinocytosis

Question for 4 Marks 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) 14) Comment on detail of Microtubule. Explain features of active transport. Explain phenomenon of osmosis. Define and explain Exocytosis. Describe microfilament. Define and explain endocytosis. Explain phagocytosis with its mechanism. Describe flagella along with functions. Explain Ca-ATPase pump. Comment on lipid bilayer model. How you will explain the primary active transport. Comparison between active and passive transport. Comparison between Endocytosis & Exocytosis. Structure of micro filament. 6
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

15)

Why Danielle model called sandwich model explain.

Question for 6 Marks 1) Explain facilited diffusion with example. 2) Explain Endocytosis with its type. 3) Describe active transport with example. 4) Describe the models of membrane.

Unit III: Biocatalysts


Q.1 Question for 2 Marks (Objective). 1) Enzymes are -------------in nature. a) c) 2) a) b) 3) a) b) 4) a) b) 5) a) b) 6) a) b) 7) a) c) 8) Acidic Basic 1 2 5 10 370-450C 100-200C Lysases Proteases Gm ketal Koshland Parlor c) d) c) d) c) d) c) d) c) d) c) d) Proteinous Neutral 3 4 6 12 600-750C 850-950C Cellulase Synthetase Farady S b) d) Emil Fishcer Arora

Enzymes are categorized in to -------------type.

The enzymes are classified into---------- major groups.

Enzyme shows maximum activity at temperature---------------

Ligases enzyme are also called as-------------

------------ is the Unit of enzyme activity

Lock and key model was proposed by-----------.

As pH of an Enzyme is increases, rate of reaction is-----------. 7


N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

a) c) 9) a) c) 10) a) c) 11) a) c) 12) a) c) 13) a) c) 14) a) c) 15)

Decrease Steady state Apo enzyme Coenzyme Biocatalyst Key of life Buchner James sumner Fumarase

b) d) b) d) b) d) b) d) b)

Increase All of the above Isozyme b&d activators all the above Kihne Duclax Chemotrypsin

The protein part of a conjugated enzyme is called as-----------

Enzymes are also called as-------------

In 1833 he word enzyme use by -----------.

----------Is a good example of Oxidoreductase class. L & D amino acid d) Succinate thiokinase Basic Neutral Copper Iron b) d) b) d) Acidic Alkaline Silver Aluminum

Enzyme from fungi & plants are active in------------condition.

------------is good example of Metalloenzymes.

A substance which bind with enzyme and bring a decrease in catalytic activity called-------------. a) c) Activator Allosteric 40- 42c 40-45c Karl Fischer Sweden Fischer 1950 1958 b) d) b) d) b) d) b) d) Inhibitor None of these 30- 35c 50-52c Emil Fischer Koshland 1953 1957

16)

Optimum temperature for most of the enzyme is between -----------. a) c)

17)

The Lock & Key model was proposed by-----------. a) c)

18)

Induced fit theory was proposed in-----------year. a) c)

19)

Koshlands model also explain the action of-------------. 8


N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

a) c) 20)

Reversible Inhibition

b)

Competitive inhibition Allosteric inhibition

Non competitive inhibition d)

Km stands for-------------constant. a) c) Koshland Menten Khune Menten b) d) Michealis Menten None of these

Question for 2 Marks (Short Answer) 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 12) 13) 14) 15) 16) 17) Give the industrial significance of Protease. Give the industrial significance of Amylase. What are Apoenzymes & coenzymes? Enlist the functions of the enzymes? What is Lineweaver Burk equation? Give the graphical presentation of the enzyme concentration. Importance of temperature in enzymology. What are the Isoenzymes? Give the functions of the enzyme in any biochemical reaction. Graphically represent effect of the pH, Temperature. What is Activator? Explain with suitable example. What is Inhibitor? Explain with suitable example Define -oxidation. Comment on Decarboxylation process. What is Transmethylation. Enlist essential and non essential amino acid. Question for 3 Marks 1) 2) 3) 4) 5) 6) 7) 8) Definition of enzymes and add a note on its types. What is the optimum temperature and the optimum pH of an enzyme? What are coenzymes? Explain their characteristics. What are the activators? What is non-competitive inhibition? How enzyme activity affect by PH? Enlist the Importance of lipase. Explain Koshlands model. 9
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

9) 10)

Comparison between competitive & non competitive inhibitors. How Substrate concentration affect on enzyme?

Question for 4 Marks 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) 14) Give the Michelis- Menten equation. What is enzyme? Add a note on its nomenclature? Explain I.U.B.? Explain the classification of the enzymes with examples? Explain the mechanism of enzyme catalysis? What are the significance of the enzyme concentration? What is enzyme inhibition? State its types. What are activators and inhibitors? Explain with suitable example. Enlist the factors affecting enzyme activity. State the applications of the proteases and the lipases. What is Enzymology? Explain the concept of biocatalysts What do you mean by essential amino acid? Add a note on biosynthesis of any one amino acid. Explain biosynthesis of Proline? Give the regulatory role of enzyme in Gluconeogenesis. Explain transamination reaction on protein.

Question for 6 Marks 1) 2) 3) 4) 5) 6) 7) 8) Give the classification of the enzymes with suitable examples Explain the enzyme-substrate complex reaction. What is optical specificity and the substrate specificity? Explain feed back inhibition? Discuss in detail -oxidation of fatty acid . Give the reaction in which oxaloacetic acid is converted in to citric acid Discuss in detail Gluconeogenesis. Explain protein degradation in details.

Unit IV: Metabolic Pathway


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Q.1 Question for 2 Marks (Objective). 1) Glycolysis, Glycogenolysis is the example of------------. a) b) 2) a) b) 3) a) b) c) d) 4) Catabolism -oxidation Glycogenolysis Glycolysis c) d) c) d) Anabolism Deamination TCA cycle Gluconeogenesis

Embeden-Mayerhoff pathway means--------------.

Transamination is the process of combination of --------&---------. Transmethylation and Methylation Deamination and Amination Decarboxylation and Carboxylation -oxidation and alpha-oxidation

Mallic acid is converted to oxaloacetic acid, in this step--------number of ATP molecules are formed. a) b) 5 3 11 8 Decarboxylation Transamination -COOH -SH essential non-essential Anabolic Catabolic c) d) c) d) c) d) c) d) c) d) c) d) 12 4 7 15 Transmethylation Deamination CH3 NH2 vitamins both a&b Metabolic Both b & d

5)

TCA cycle involve----------no of enzymes. a) b)

6)

Glutamate Pyruvate transaminase is used in---------a) b)

7)

In Decarboxylation reaction, CO2 is removed from----------group. a) b)

8)

Valine is present in------------amino acid. a) b)

9)

Glycolysis is a----------- process. a) b)

10)

Alpha ketoglutaric D hydrogenase complex is formed in------------. a) Glycolysis c) 11 Decarboxylation


N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

b) a) c) a) c)

Transmethylation 80-90% 40-55%

d) b) d)

Kreb Cycle 65-70% 50-60% b) pyroline-5-carboxylate

11) ---------of the ATP is synthesized in Kreb cycle

12) Homocystein condenses with serine to form------------. glutamate- 5-semialdehyde. Cystathionine d) none of these

Question for 2 Marks (Short Answer) 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) Give an Importance of Essential amino acids. Mention the function of S-Adenosyl methionine. Give the pathway of Gluconeogenesis. Explain the role of Glucokinase Explain-Cori Cycle. Give the importance of Glycolysis cycle. What is Transamination? Diagramatically represent the TCA Cycle. Enlist the stages where ATP formation takes place in TCA Cycle. What is Oxidative Deamination?

Question for 3Marks. 1) 2) 3) 4) 5) Give the features of Transamination. Give the role of Glutamate dehydrogenase. Give the list of enzymes involved in TCA Cycle. What are Essential & Non essential amino acids? Give the importance of catabolic pathway.

Question for 4 Marks. 1) 2.) 3) 4) 5) Give the biosynthesis of Glycine. What is Decarboxylation? Give the features of Transmethylation. Importance of ED Pathway. Give the biosynthesis of Proline.
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

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6) 7) 8) 9) 10)

Give the mechanism of Transamination. What is the Non Oxidative Deamination? Give the significance of Transmethylation. Give the importance of Gluconeogenesis. In which location Gluconeogenesis occurs and give the importance of Gluconeogenesis.

Question for 6 Marks. 1) 2) 3) 4) 5) Give the Energetics of TCA Cycle. Give the Energetics of Glycolysis Cycle. Explain the sequence of -Oxidation. Explain the synthesis of S-Adenosyl methionine. What is Catabolism? Explain an account of Glycolysis.

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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

NORTH MAHARASHTRA UNIVERSITY, JALGAON


QUESTION BANK OF BIOTECHNOLOGY

CLASS- S.Y.B.Sc SEMESTER-I PAPER: BT 212- MOLECULAR BIOLOGY Unit I: Genome Organization
Q.1 Question for 2 Marks (Objective). 1) The most conserved histones are. a) c) 2) a) c) 3) a) C) 4) a) c) 5) a) c) 6) a) c) 7) a) c) 8) H1 & H2A H3 & H4 Nucleus Nucleolus UAG AUG anticodon codon Meiosis Mitosis Chromosome Chromatin Introns Exon b) c) b) d) b) d) b) d) b) d) b) d) b) d) H2A & H2B H1 & H4. Cytoplasm Nucleoid. AUC GUA. Synonyms Stop codon. Interphase M-Phase Nucleoprotein None. Stop sequence None.

The E-coli circular DNA packaged into region of cell called.

The prokaryotic translation start with initiation codon.

The triplet of bases present on specific t-RNA molecules are

The chromatin is more dispersed during.

The nuclear DNA-protein complex is called..

are non coding sequence present in m-RNA molecules.

is due to less stringent pairing of third base of codon with anticodon. a) c) Degeneracy Wobbling b) d) Mutation Universality.

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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

9)

The sequence of m-RNA transcribed & translated is known as. a) c) Non coding sequence Mid sequence b) d) Exon Intron

10)

.. is the distinct sequence of a DNA molecule forming part of chromosome. a) c) Gene Nucleotide b) d) Chromatin. Genome.

11)

Nucleosome core particle contains a double stranded DNA fragment of base pairs. a) c) 148 156 b) d) 144 146.

Q.2 Question for 2 Marks (Short answer). 1) 2) 3) 4) 5) 6) 7) 8) 9) Define Nucleosomes. Explain Histones protein? Comment on concept of Gene. Define Intron. Comment on Exon as an important part of m-RNA. Explain role of Non Histone proteins. Define a) Chromatin b) Chromosome Define Genetic code & Codon. Explain degeneracy of genetic code.

Q.3 Question for 3 Marks 1) 2) 3) 4) 5) Explain how Histine protein is important in DNA packaging? What is Intron? Explain its types. Comment on propeties of genetic code. Discuss nucleosomes as fundamentle unit of DNA organization. Comment on organization of Chromatin.

Q.4Question for 4 Marks 1) 2) Distinguish between Histone & Non histone proteins. Explain Degeneracy & wobbling of genetic code. 15
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

3) 4) 5) 6)

Explain detail structure of Nucleosome. Discuss the importance of chromatin organization. What is gene? Explain concept of gene briefly. Compare: Chromatin organization in Prokaryote & Eukaryote.

Q.5 Question for 6 Marks. 1) 2) 3) 4) Describe nature & properties of genetic code. What is splicing? Explain Intron with self splicing activity. What is Chromatin? Explain its organizatin. Explain the process of nucleosome formation.

Unit II: DNA Replication & Damage


Q.1 Question for 2 Marks (Objective). 1) .. enzyme relaxes the supercolling of double stranded DNA molecule a) c) 2) DNA Polymerase DNA helicase b) d) Topoisoemerase DNA Ligase

The agents that are responsible for bringing variation in genetic message, known as . a) c) Unusual bases Mutagen Beadle Kornberg Nitrous Acid Acetic Acid b) d) b) Tautomers d) b) d) Isomers Tatum Edman

3)

DNA polymerase I enzyme was isolated by a) c)

4)

react with bases that contain amino group for mutation. a) c) Nitric Acid Ammonium Nitrate

5)

DNA photolyse enzyme absorbs light of wavelength ranging from to . nm. a) c) 100 to 300 350 to 450 dna B protein b) d) b) 200 to 300 300 to 500 dna G protein

6)

RNA primers are synthesized by a template independent enzyme . a)

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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

c) 7)

DNA polymerase-I

d)

Topoisomerases

Replacement of a purine residue by a pyrimidine residue, the effect termed as a) c) Mutation Transversion 1000 10000 part of DNA b) d) b) d) b) d) b) d) b) d) b) d) Substitution mutation Transition 100 10 polymeraseIII clamp loader clamp DNA photolyse AP endonuclease tus ter Nucleotide excision repair Base excision repair enzyme confers

8)

DNA polymerase III add about nucleotide / sec. a) c)

9)

processivity a) c)

core enzyme both a & b DNA glycolyses DNA ligase stop single strand binding Mismatch repair Direct repair

10)

In base excision repair enzyme removes unusual bases. a) c)

11)

protein brings termination of DNA replication. a) c)

12)

is known as long patch repair. a) c)

Q.2 Question for 2 marks each 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) Define leading & lagging strand. Explain role of DNA helicase. Comment on action on DNA ligase. Explain termination event in DNA replication. Define substitution mutation with sub types. Draw a diagram of Okazaki fragment formation. Comment on role of dnaA & dnaB protein in DNA replication. Explain briefly process of Alkylation. Comment on direct repair mechanism. Give role of DNA glycolyses & AP endonuclease in base excision repair. 17
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

Q.3 Question for 3 marks each 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) 11) What is oxidative deamination? Explain it. Explain activities of DNA polymerase - I Describe Okazaki fragment formation. Comment on Direct repair mechanism. Define Mutation & mutagenic agent Compare: Natural & Artificial mutation. Write a note on structure of DNA polymerase - III Explain the initiation event in prokaryotic DNA replication. Define Chemical & Physical mutagen. Add a note on DNA ligase. Comment on alkylation as chemical mutation. Explain role of DNA helicase & single strand binding protein in DNA replication.

12)

Q.4 Question for 4 marks. 1) 2) 3) 4) 5) 6) 7) 8) Describe formation of Okazaki fragment. Comment on formation of pysimidine dimer Describe base excision repair Write a note on structure & function of DNA polymerase - I What is mutation? Describe oxidative deamination. Explain the role of primer & template in DNA replication. Comment on mismatch repair Add a note on Nucleotide excision repair.

Q.5 Question for 6 marks. 1) 2) 3) 4) Enlist the enzymes involved in prokaryotic DNA replication & comment on their function. Comment on initiation, elongation & termination events in prokaryotic DNA replication. Describe long patch repair mechanism. What is physical mutagen? Comment on pyrimidine dimer formation. 18
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

5)

Distinguish between DNA polymerase I & DNA polymerase II.

Unit III: Central dogma of Molecular Biology


Q.1 Question for 2 Marks (Objective). 1) Which of the enzyme is involved in Transcription. a) c) 2) a) c) 3) a) c) 4) a) c) 5) a) c) 6) a) c) 7) a) c) 8) DNA Polymerase b) RNA Polymerase d) both b and c Amino acyl tRNA transferase t-RNA r RNA Guanine Uracil AUG UGA N formyl methionine glycine 50s and 30s 40s and 30s DNA Polymerase peptidyl transferase b) d) b) d) b) d) b) d) b) d) b) d)

..RNA is exist in high amount in cell. m RNA none. Cytosine Adenine. UAG UAA. alanine Leucine. 60s and 40s 60s and 10s Amino acyle tRNA synthatase both band c.

Thymine in DNA is replaced by nucleiotide in RNA.

is the starting codon in translation.

.is the first amino acid in proteins of bacteria.

70S ribosome of bacteria are made up ofand.subunits.

Activation of amino acid is carried out by enzyme.

EF Tu and EF Ts complex of proteins are involved in step of translation. a) c) Initiation Activation b) d) Elongation Termination.

9)

IF 150 ribonucleotides are present on mRNA, hence.. number of amino acids on the protein. a) c) 75 100 b) d) 50 150.

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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

10)

In eukaryotes enzyme involved in synthesis of mRNA in transcription. a) c) RNA pol 1 RNA pol 3 b) d) RNA pol2 none.

Q.2 Question for 2 Marks (Short answer). 1) 2) 3) 4) 5) 6) 7) 8) Define transcription and what is the role of sigma factor. Define translation and add a note on initiation and termination codon. What is the role of RNA polymerase? Draw the structure of mRNA and explain it. Explain 80s ribosome of eukaryotes. Write a note on initiation of translation. Define transcription and translation. Write a short note on 70s ribosome. Q.3 Question for 3 Marks 1) 2) 3) 4) 5) Explain the structure of RNA. Write a short note on: a)Initiation codon b)termination codon. What is the role of t-RNA in translation? Write the short note on structure of ribosome. Distinguish between 70s and 80s ribosome.

Q.4 Question for 4 Marks 1) 2) 3) 4) 5) 6) 7) 8) How protein elongation take place in translation? Describe the process of translation termination? Write a note on activation of amino acids. Explain the difference between transcription and translation. Explain the process of transcription. Explain the structure of 70s and 80s ribosome. Explain the role of a) IF1 b) IF2 c) IF 3 d) EF Tu & EF Ts e) RF Distinguish between transcription and translation.

Q.5 Question for 6 Marks 1) Explain the different properties of genetic code.
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

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2) 3) 4)

Explain the function of tRNA ,mRNA and rRNA. Give an account of elongation process of translation. Write a note on transcription.

Unit IV: Regulation of Gene Expression


Q.1 Question for 2 Marks (Objective). 1) . is a DNA sequence that regulates transcription of structural genes. a) c) 2) a) c) 3) a) c) 4) a) c) 5) a) c) 6) a) c) 7) a) c) 8) a) c) 9) a) Regulatory site Operator site Protein coding genes Non coding genes Inhibitor Repressor Lactose ATP Stringent control Positive control Repressor molecule Regulatory enzymes Operator Regulator Polycistronic Dicistronic Galactosidase b) d) b) d) b) d) b) d) b) d) b) d) b) d) b) d) b) Promoter site Repressor site. Structural genes none. Activator Controller. cAMP Allolactose. Negative control None. Inducer proteins Activator molecule. Binding site Promoter. Monocitronic Multivalent. Galactosidase.
N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB

Operon consists of .. cluster.

Regulatory protein is also known as ... of operon.

is an inducer of the lac operon.

The lac operon is a good example of ...

Structural genes of operon encodes for

. Is binding site of RNA polymerase on sequence of DNA.

.. type of mRNA transcribed by RNA pol. In Lac operon.

The enzyme..hydrolyzes lactose to glucose & galactose.

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c) 10) a) c)

Lactose permease Beadle & Tatum Jacob & Monad

d) b) d)

lac convertase Broom & Gillbert Richadr & Philip.

Concept of Operon wag given by .&..

Q.2 Question for 2 Marks 1) 2) 3) 4) 5) 6) 7) 8) 9) 10) Give the role of three enzyme of Lac-operon. Comment on importance of cAMP in Lac operon. What are structural genes? Explain their role. Define Promoter & Operator. What is operon? Explain its concept briefly. Compare positive & negative regulation. Give the role of allolactose in lac operon. Give the importance of regulatory genes. Enlist enzymes of lac operon & comment on their role. Define polycistronic mRNA.

Q.3 Question for 3 Marks. 1) 2) 3) 4) 5) 6) 7) 8) Comment on concept of operon. What is structural gene? Explain in details. Describe Regulatory gene? Comment on Lac repressor protein. Explain promoter & operator of operon. Compare Polycistronic & Monocistronic mRNA. Give significance of an Inducer in Lac operon. Define Operon? Enlist Enzymes of Lac operon with their role.

Q.4 Question for 4 Marks. 1) 2) 3) 4) 5) Distinguish between Positive & Negative Regulation. Comment on Regulation of operon. What is Promoter? Explain its Components. Explain Catabolite repression. Describe operator & structural gene.

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Q.5 Question for 6 Marks 1) 2) 3) 4) Describe the detail mechanism of Lac operon. Comment on impotrance of Catabolite activator protein in lac operon functioning. Explain repression & induction mechanism of Lac operon. Describe in detail regulation of Lac operon.

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N.M.U. / Life Sciences / S.Y.BSc. BT-211 QB-2008/ HMB