Exam Details
Subject | bioenergetics and enzymology | |
Paper | ||
Exam / Course | b.sc. (biotechnology) | |
Department | ||
Organization | solapur university | |
Position | ||
Exam Date | March, 2018 | |
City, State | maharashtra, solapur |
Question Paper
B.Sc. II (Biotechnology) (Semester III) (CBCS) Examination, 2018
bioenergetics and enzymology
Day and Date Saturday, 28-04-2018 Max. Marks 70
Time 2.30 p.m. to 5.00 p.m.
Instructions All questions carry equal marks.
Figures to right indicate full marks.
Draw neat and labeled diagrams.
1. Rewrite the following sentences by using correct alternative 14
According to second law of thermodynamics, entropy of a closed universal
system always
Decreases Increases
Remains constant Disappears
In cleavage, one of the atoms retains both bonding
electrons after bond breakage.
Homolytic Internal
Heterolytic Catalytic
The free energy of ATP hydrolysis under standard conditions is
KJ/mol.
2.303 51.8 8.314 30.5
The quantitative expression of randomness of a system is
Enthalpy Entropy
Mass action Free energy
In the reaction Fe2+ → Fe3+ e
Fe2+ is the electron donor
Fe2+ is the electron acceptor
Fe3+ is the electron donor
Fe+ is the electron donor
In type of inhibition, the inhibitor molecule binds with the
transition state.
Competitive Noncompetitive
Uncompetitive Irreversible
The molecule is used as energy currency in biological
systems.
ATP ADP TTP GDP
The molecule gets upon accepting electron.
Reduced Oxidized
Phosphorylated Hydrolyzed
Enzymes are assigned with number for their
classification as per IUB.
IUB IC EC IUPAC
10) The protein part an enzyme is
Cofactor Modulator
Apoenzyme Holoenzyme
11) is the concentration where v Vmax/2.
Δ H Vmax Δ G Km
12) Abzymes are the catalytic
RNA DNA Antibodies Proteins
13) The enzyme activity per milligram of protein is known as
Absolute activity Specific activity
Turnover number Weighed activity
14) The minimum energy barrier required to attain for catalysis is
Free energy
Activation energy
Total energy
Binding energy
2. Answer the following (any 14
Write about biological standard state.
ii) Write about mass action ratio of reaction.
iii) What is standard free energy change
Set P
*SLRSA26* SLR-SA 26
iv) Write a note on mode of enzyme action.
State the relationship between equilibrium constant and free energy
change.
vi) Define redox potential. Write its unit.
vii) Write about aldol condensation.
viii) Write any two clinical significances of LDH.
ix) Write about induced fit hypothesis of enzyme action.
3. Answer the following (any 10
Explain free energy concept. How free energy change can be determined
ii) Describe group transfer reactions.
iii) Write about thermodynamic systems. State first and second law of
thermodynamics.
Write a note on line-weaver burk plot and its limitations. 4
4. Answer any two of the following 14
Write an account on factors affecting enzyme activity.
ii) Describe regulation of enzymes in living system.
iii) Derive Michaelis Menten equation.
5. Answer any two of the following 14
Give detailed classification of enzymes with example of each class.
ii) Describe biological half reactions. Add a note on measurement of redox
potential.
iii) Explain in detail competitive, uncompetitive and non-competitive
inhibition.
bioenergetics and enzymology
Day and Date Saturday, 28-04-2018 Max. Marks 70
Time 2.30 p.m. to 5.00 p.m.
Instructions All questions carry equal marks.
Figures to right indicate full marks.
Draw neat and labeled diagrams.
1. Rewrite the following sentences by using correct alternative 14
According to second law of thermodynamics, entropy of a closed universal
system always
Decreases Increases
Remains constant Disappears
In cleavage, one of the atoms retains both bonding
electrons after bond breakage.
Homolytic Internal
Heterolytic Catalytic
The free energy of ATP hydrolysis under standard conditions is
KJ/mol.
2.303 51.8 8.314 30.5
The quantitative expression of randomness of a system is
Enthalpy Entropy
Mass action Free energy
In the reaction Fe2+ → Fe3+ e
Fe2+ is the electron donor
Fe2+ is the electron acceptor
Fe3+ is the electron donor
Fe+ is the electron donor
In type of inhibition, the inhibitor molecule binds with the
transition state.
Competitive Noncompetitive
Uncompetitive Irreversible
The molecule is used as energy currency in biological
systems.
ATP ADP TTP GDP
The molecule gets upon accepting electron.
Reduced Oxidized
Phosphorylated Hydrolyzed
Enzymes are assigned with number for their
classification as per IUB.
IUB IC EC IUPAC
10) The protein part an enzyme is
Cofactor Modulator
Apoenzyme Holoenzyme
11) is the concentration where v Vmax/2.
Δ H Vmax Δ G Km
12) Abzymes are the catalytic
RNA DNA Antibodies Proteins
13) The enzyme activity per milligram of protein is known as
Absolute activity Specific activity
Turnover number Weighed activity
14) The minimum energy barrier required to attain for catalysis is
Free energy
Activation energy
Total energy
Binding energy
2. Answer the following (any 14
Write about biological standard state.
ii) Write about mass action ratio of reaction.
iii) What is standard free energy change
Set P
*SLRSA26* SLR-SA 26
iv) Write a note on mode of enzyme action.
State the relationship between equilibrium constant and free energy
change.
vi) Define redox potential. Write its unit.
vii) Write about aldol condensation.
viii) Write any two clinical significances of LDH.
ix) Write about induced fit hypothesis of enzyme action.
3. Answer the following (any 10
Explain free energy concept. How free energy change can be determined
ii) Describe group transfer reactions.
iii) Write about thermodynamic systems. State first and second law of
thermodynamics.
Write a note on line-weaver burk plot and its limitations. 4
4. Answer any two of the following 14
Write an account on factors affecting enzyme activity.
ii) Describe regulation of enzymes in living system.
iii) Derive Michaelis Menten equation.
5. Answer any two of the following 14
Give detailed classification of enzymes with example of each class.
ii) Describe biological half reactions. Add a note on measurement of redox
potential.
iii) Explain in detail competitive, uncompetitive and non-competitive
inhibition.
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