Exam Details
Subject | bioenergetics and enzymology (old) | |
Paper | ||
Exam / Course | b.sc. (biotechnology) | |
Department | ||
Organization | solapur university | |
Position | ||
Exam Date | October, 2018 | |
City, State | maharashtra, solapur |
Question Paper
B.Sc. II (Biotechnology) (Semester IV) (CGPA)
Examination, 2018
bioenergetics and enzymology
Day and Date Wednesday, 12-12-2018 Total Marks 70
Time 10.30 a.m. to 1.00 p.m.
Instructions All questions carry equal marks.
Figures to right indicate full marks.
Draw neat and labeled diagrams wherever necessary.
1. Rewrite the following sentences by using correct alternative. 14
Half cells contain two ions of same element with different
Atomic mass Oxidation state
Nucleon number Electronic configuration
Negative electrode in half cell is made up of
Hydrogen Zinc Copper Tungsten
The enzyme which forms the peptide bond is known as
Carbonic unhydrase Peptidase
Carbohydrase Peptidyl transferase
The catalytic efficiency of two distinct enzymes can be compared based on factor.
Km Product formation
Size of the enzymes pH of optimum value
Inhibition of enzyme cytochrome oxidase by carbon monoxide is an example for
Feed back inhibition Competitive inhibition
Non competitive inhibition Uncompetitive
In non-competitive inhibition extent of inhibition depends only on
Concentration of enzyme
Concentration of substrate
Concentration of inhibitor
Concentration of ES complex
In uncompetitive inhibition inhibitor binds only to
Enzyme Substrate
ES-complex Active site
When V and P values are constant in biochemical system Δ H
Δ S Δ T Δ Q Δ E
The number of isoenzyme forms of alcohol dehydrogenose in maize are
4 8 12 16
10) The required pH for action of trypsin is
5 6 7 8
11) A qualitative composition of product's molecule is completely identical to substrate's one, but the structure is different. Name the enzyme class.
Isomerase Hydrolase
Lyase Ligase
12) Coenzyme carboxybiotin is the derivative of vitamin
B1 B2 B3 B7
13) Inhibitor of succinate dehydrogenase is
Sulfa drugs Cyanides
Succinic acid Malonic acid
14) Released kinetic energy by breakdown of enzymes is stored in bonds of ATP molecules in form of
Potential energy Kinetic energy
Hydra energy Thermal energy
2. Answer the following (any 14
What is inhibitor give its one example
ii) Give two examples of coenzyme and prosthetic group.
iii) Define entropy and enthalpy.
iv) What is the significance of km and Vmax
Define abzymes.
vi) What is the unit of enzyme activity and specific activity
vii) Draw the structure of ATP.
viii) Write a note on mass action ratio of reaction.
ix) Define cofactor with one example.
3. Answer the following (any 10
Explain first and second law of thermodynamics.
ii) Write a note on biological half reactions.
iii) How the substrate concentration affects the enzyme activity
Explain concept of activation energy in enzyme catalysed reaction. 4
4. Answer any two of the following 14
Derive of Michaelis-Menten equation for single substrate.
ii) Explain relationship between equilibrium constant and standard free energy change.
iii) Write a note on classification system of enzyme with example of each class.
5. Answer any two of the following 14
Write a note on types of enzyme inhibition with their kinetics.
ii) Explain regulation of enzyme in living system.
iii) Write a note on standard redox potential and free energy change.
Examination, 2018
bioenergetics and enzymology
Day and Date Wednesday, 12-12-2018 Total Marks 70
Time 10.30 a.m. to 1.00 p.m.
Instructions All questions carry equal marks.
Figures to right indicate full marks.
Draw neat and labeled diagrams wherever necessary.
1. Rewrite the following sentences by using correct alternative. 14
Half cells contain two ions of same element with different
Atomic mass Oxidation state
Nucleon number Electronic configuration
Negative electrode in half cell is made up of
Hydrogen Zinc Copper Tungsten
The enzyme which forms the peptide bond is known as
Carbonic unhydrase Peptidase
Carbohydrase Peptidyl transferase
The catalytic efficiency of two distinct enzymes can be compared based on factor.
Km Product formation
Size of the enzymes pH of optimum value
Inhibition of enzyme cytochrome oxidase by carbon monoxide is an example for
Feed back inhibition Competitive inhibition
Non competitive inhibition Uncompetitive
In non-competitive inhibition extent of inhibition depends only on
Concentration of enzyme
Concentration of substrate
Concentration of inhibitor
Concentration of ES complex
In uncompetitive inhibition inhibitor binds only to
Enzyme Substrate
ES-complex Active site
When V and P values are constant in biochemical system Δ H
Δ S Δ T Δ Q Δ E
The number of isoenzyme forms of alcohol dehydrogenose in maize are
4 8 12 16
10) The required pH for action of trypsin is
5 6 7 8
11) A qualitative composition of product's molecule is completely identical to substrate's one, but the structure is different. Name the enzyme class.
Isomerase Hydrolase
Lyase Ligase
12) Coenzyme carboxybiotin is the derivative of vitamin
B1 B2 B3 B7
13) Inhibitor of succinate dehydrogenase is
Sulfa drugs Cyanides
Succinic acid Malonic acid
14) Released kinetic energy by breakdown of enzymes is stored in bonds of ATP molecules in form of
Potential energy Kinetic energy
Hydra energy Thermal energy
2. Answer the following (any 14
What is inhibitor give its one example
ii) Give two examples of coenzyme and prosthetic group.
iii) Define entropy and enthalpy.
iv) What is the significance of km and Vmax
Define abzymes.
vi) What is the unit of enzyme activity and specific activity
vii) Draw the structure of ATP.
viii) Write a note on mass action ratio of reaction.
ix) Define cofactor with one example.
3. Answer the following (any 10
Explain first and second law of thermodynamics.
ii) Write a note on biological half reactions.
iii) How the substrate concentration affects the enzyme activity
Explain concept of activation energy in enzyme catalysed reaction. 4
4. Answer any two of the following 14
Derive of Michaelis-Menten equation for single substrate.
ii) Explain relationship between equilibrium constant and standard free energy change.
iii) Write a note on classification system of enzyme with example of each class.
5. Answer any two of the following 14
Write a note on types of enzyme inhibition with their kinetics.
ii) Explain regulation of enzyme in living system.
iii) Write a note on standard redox potential and free energy change.
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