Solapur University
B.Sc. – II (Biotechnology) (Semester – III) (Old) Examination, 2015
BIOENERGETICS AND METABOLISM – I
(Bioenergetics and Thermodynamics)
Day and Date : Thursday, 7-5-2015 Max. Marks : 50
Time : 3.00 p.m. to 5.00 p.m.
N. B. : 1) All questions are compulsory.
2) Draw neat labelled diagram wherever necessary.
3) Figures to the right indicate full marks.
1. Write the following sentences by selecting the most correct answer from given
options. 10
1) If free energy of a system is negative, then the reaction is _________
a) Exergonic b) Endergonic
c) Equilibrium d) Spontaneous
2) __________ is the nonprotein part of a conjugated enzyme required for
biological activity.
a) Holoenzyme b) Cofactor
c) Isoenzyme d) Apoenzyme
3) __________ enzyme can hydrolyze the glycosidic bonds in peptidoglycan
compounds.
a) Lysozyme b) Carboxypeptidase
c) Chymotrypsin d) Amylase
4) Lineweaver-Burk plot is a graph of
a) [ ] S
1 V Vs b) V [ ] S
V
1
s
c) [ ] S
1 V
V
1
s d) [V] Vs[S]
SLR-M – 33 -2-
5) Thiamine pyrophosphate [TPP] is the biologically active form of vitamin ______
a) B – 1 b) B – 2
c) B – 3 d) B – 12
6) The structure of inhibitor closely resembles the structure of substrate in
____________ enzyme inhibition.
a) Allosteric b) Uncompetitive
c) Noncompetitive d) Competitive
7) The rates of ____________ order reactions do not vary with increasing or
decreasing reactant concentrations.
a) First b) Second
c) Third d) Zero
8) A system that neither exchanges energy nor matter with its surroundings is
called as ___________ system.
a) Open b) Closed
c) Isolated d) Negative
9) _________ is the measure of randomness of a system.
a) Enthalpy b) Entropy
c) Free energy d) Vmax
10) More __________ the reduction potential, more is the affinity of the species
for electrons.
a) Negative b) Passive
c) Positive d) Active
2. Answer any five of the following : 10
1) State the relationship between equilibrium constant and standard free energy
change.
2) What are limitations of Lineweaver-Burk plot ?
3) Define enzyme activity. How can it be measured ?
4) What is free energy of hydrolysis of ATP ?
5) Differentiate between reversible and irreversible enzyme inhibition.
6) What is entropy ? State second law of thermodynamics.
-3- SLR-M – 33
3. A) Answer any two of the following : 6
1) What are the different applications of thermodynamics in biochemistry ?
2) Explain enzyme catalysis on the basis of strain and distortion theory.
3) What is order of a reaction ? Give kinetics of zero order reaction.
B) Describe the mechanism of action of chymotrypsin. 4
4. Answer any two of the following : 10
1) Describe the phosphate group transfer by high energy phosphate compounds.
2) Discuss the effect of different physicochemical factors on enzyme activity.
3) Derive the Michaelis Menten equation for unisubstrate reactions. State the
significance of Km.
5. Answer any two of the following : 10
1) Write an account on ‘enzyme inhibition’.
2) Write a note on thermodynamic systems and state functions.
3) Describe biological oxidation reduction reactions. Add a note on ‘redox potential’.
B.Sc. – II (Biotechnology) (Semester – III) (Old) Examination, 2015
BIOENERGETICS AND METABOLISM – I
(Bioenergetics and Thermodynamics)
Day and Date : Thursday, 7-5-2015 Max. Marks : 50
Time : 3.00 p.m. to 5.00 p.m.
N. B. : 1) All questions are compulsory.
2) Draw neat labelled diagram wherever necessary.
3) Figures to the right indicate full marks.
1. Write the following sentences by selecting the most correct answer from given
options. 10
1) If free energy of a system is negative, then the reaction is _________
a) Exergonic b) Endergonic
c) Equilibrium d) Spontaneous
2) __________ is the nonprotein part of a conjugated enzyme required for
biological activity.
a) Holoenzyme b) Cofactor
c) Isoenzyme d) Apoenzyme
3) __________ enzyme can hydrolyze the glycosidic bonds in peptidoglycan
compounds.
a) Lysozyme b) Carboxypeptidase
c) Chymotrypsin d) Amylase
4) Lineweaver-Burk plot is a graph of
a) [ ] S
1 V Vs b) V [ ] S
V
1
s
c) [ ] S
1 V
V
1
s d) [V] Vs[S]
SLR-M – 33 -2-
5) Thiamine pyrophosphate [TPP] is the biologically active form of vitamin ______
a) B – 1 b) B – 2
c) B – 3 d) B – 12
6) The structure of inhibitor closely resembles the structure of substrate in
____________ enzyme inhibition.
a) Allosteric b) Uncompetitive
c) Noncompetitive d) Competitive
7) The rates of ____________ order reactions do not vary with increasing or
decreasing reactant concentrations.
a) First b) Second
c) Third d) Zero
8) A system that neither exchanges energy nor matter with its surroundings is
called as ___________ system.
a) Open b) Closed
c) Isolated d) Negative
9) _________ is the measure of randomness of a system.
a) Enthalpy b) Entropy
c) Free energy d) Vmax
10) More __________ the reduction potential, more is the affinity of the species
for electrons.
a) Negative b) Passive
c) Positive d) Active
2. Answer any five of the following : 10
1) State the relationship between equilibrium constant and standard free energy
change.
2) What are limitations of Lineweaver-Burk plot ?
3) Define enzyme activity. How can it be measured ?
4) What is free energy of hydrolysis of ATP ?
5) Differentiate between reversible and irreversible enzyme inhibition.
6) What is entropy ? State second law of thermodynamics.
-3- SLR-M – 33
3. A) Answer any two of the following : 6
1) What are the different applications of thermodynamics in biochemistry ?
2) Explain enzyme catalysis on the basis of strain and distortion theory.
3) What is order of a reaction ? Give kinetics of zero order reaction.
B) Describe the mechanism of action of chymotrypsin. 4
4. Answer any two of the following : 10
1) Describe the phosphate group transfer by high energy phosphate compounds.
2) Discuss the effect of different physicochemical factors on enzyme activity.
3) Derive the Michaelis Menten equation for unisubstrate reactions. State the
significance of Km.
5. Answer any two of the following : 10
1) Write an account on ‘enzyme inhibition’.
2) Write a note on thermodynamic systems and state functions.
3) Describe biological oxidation reduction reactions. Add a note on ‘redox potential’.
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