M.Sc. DEGREE EXAMINATION, NOVEMBER 2017
Third Semester
Bioinformatics
STRUCTURAL BIOLOGY
(CBCS 2016 onwards)
Time 3 Hours Maximum 75 Marks
Part A (10 x 2 20)
Answer all questions.
1. Draw a unit cell of your choice and point out cell
parameters.
2. Define centre of inversion with a diagrammatic example.
3. What is the major advantage of a "neutron diffraction"
study of crystals?
4. Why Radio frequency is used in NMR?
5. Reason out for referring crystallization reagents as
precipitating solutions.
6. What is the radius of Ewald's sphere?
7. Mention any two restriction enzymes.
8. Expand MIR and MAD.
Sub. Code
502302
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9. Why "R-factor" are referred as Reliability index?
10. Define Vander Waals radii.
Part B x 5 25)
Answer all questions choosing either or
11. Explain space group P2 with proper notations,
equivalent positions.
Or
Write Fourier equation to calculate electron density
and explain.
12. Appreciate the principle and usage of free electron
laser technology in structure Biology.
Or
Discuss applications of NMR in structure Biology.
13. Explain Lorentz correction used in Data reduction
procedures.
Or
Explain Patterson method of solving crystal
structure.
14. Explain Hanging drop of crystallization practiced to
crystallize proteins.
Or
Discuss Ramachandran plot for its role in structural
Biology.
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15. Explain all possible conformations assumed by fully
saturated six membered ring structure.
Or
Explain torsion angle and how to calculate such
parameter.
Part C x 10 30)
Answer any three questions.
16. Derive Bragg's law and discuss in detail.
How "Phase problem" arises.
17. Appreciate cryo electron microscopy for protein
assembly analysis.
Describe special features that can be used for
structural biology problems.
18. Explain the assumptions of Direct Methods.
Discuss least squares procedure adapted during
structure refinement.
19. Explain molecular replacement to determine 3D
structure of a protein.
20. Discus in detail about various conformational aspects in a
riven protein structure.
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