M.Sc-M.Sc Bio Chemistry 1st Sem BCH - 171 : Enzymology and Biophysical Techniques(University of Pune, Pune-2013)
M.Sc. (Semester - I)
BIOCHEMISTRY
SEAT No. :
[Total No. of Pages : 2
BCH - 171 : Enzymology and Biophysical Techniques
(2010 Pattern)
Time : 3 Hours] [Max. Marks : 80
Instructions to the candidates :
1) All questions are compulsory.
2) Answers to both the sections should be written in separate answer books.
3) Figures to the right indicate full marks.
SECTION - I
(Enzymolgy)
Q1) Answer any three of the following : [15]
a) What is substrate cycle? Explain with suitable example.
b) Discuss and two factors leading to rate enhancement of enzyme catalyzed
reactions.
c) Explain the mechanism of action of triosephosphate isomerase.
d) Define the terms :
i) apoenzyme ii) holoenzyme
iii) allosteric site iv) cofactor
Q2) Answer any three of the following : [15]
a) Discuss in detail effect of substrate concentration on enzyme catalyzed
reaction.
b) Explain the various conditions under which the enzyme-substrate complex
is stabilized to determine the mechanism of enzyme catalysis by X-ray crystallography.
c) How activity of an enzyme is regulated by irreversible changes in covalent
structure? Explain with example.
d) Study of pre-steady state kinetics determines the mechanism of enzyme
catalysis. Explain.
P.T.O.
Q3) Answer any two of the following : [10]
How the rate of degradation (Kd) of the enzyme is measured?
What is positive co-operativity? Explain with suitable example.
Why is chymotrypsin most active at pH 8? Explain its mechanism.
SECTION - II
(Biophysical Techniques)
Q4) Answer any three of the following. [15]
a) Describe DNA cellulose and MAK chromatography.
b) Write a note on SDS-PAGE.
c) How does HPTLC give rapid separation and higher resolution?
d) What do you understand the term ‘finger-printing’? List out its application.
Q5) Answer any three of the following : [15]
Draw the schematic diagram of a UV-VIS spectrometer and explain the
instrumentation.
Explain the principle and application of Hydroxyapatite Chromatography.
How can molecules with the same charge at varying amounts be separated
by chromatography?
Explain any two applications of dialysis.
Q6) Answer any two of the following : [10]
What are the applications of purified enzymes? How enzymes are
separated on the basis of their solubility?
How molecular weight of a protein can be determined by gel
chromatography.
What is restriction mapping? Explain with suitable example.
Earning: Approval pending. |