Exam Details

Subject structural biology
Paper
Exam / Course m.sc bioinformatics
Department
Organization alagappa university
Position
Exam Date April, 2016
City, State tamil nadu, karaikudi


Question Paper

M.Sc. DEGREE EXAMINATION, APRIL 2016
Second Semester
Bio Informatics
STRUCTURAL BIOLOGY
(2013 onwards)
Time 3 Hours Maximum 75 Marks
Part A (10 2 20)
Answer all questions.
All questions carry equal marks.
1. Mention the main difference between a crystal and
amorphous material.
2. How atomic scattering factor and atomic number are
related?
3. What is the advantage of Cryo electron microscopy over
regular electron microscopy?
4. What is an NMR inactive nuclei?
5. Mention any two crystallization methods.
6. Appreciate one important role of rDNA technology in
protein chemistry research.
7. Expand MIR, SIR, MR and SAD.
8. How to discriminate a protein crystal from a salt crystal?
Sub. Code
502202
RW-10865
2
Wk6
9. Define "Torsional Angle"
10. Mention any two non-covalent interactions with energy
preference.
Part B 5 25)
Answer all questions choosing either or
All questions carry equal marks.
11. Discuss about Crystal systems.
Or
Explain the concept of Structure Factor.
12. Why water cannot be used in NMR studies and
what are the solvent preferences?
Or
How to validate a structure particularly a protein
structure.
13. What are steps involved in X-ray diffraction data
reduction for single crystals.
Or
Discuss: The working principle of "Patterson
Method".
14. Differentiate soaking and co-crystallization for their
advantages and limitations.
Or
Write a note on "Synchrotron Radiation".
15. Define a torsion angle and its use in determining
conformation in a given molecule of your choice.
Or
Discuss in detail about hydrogen bond and describe
C-H...O and N-H... interactions.
RW-10865
3
Wk6
Part C 10 30)
Answer any three questions.
All questions carry equal marks.
16. Explain the space groups P21 and P21/c with clear
necessary diagrams.
17. How NMR is used to understand the structure of a
protein by native and isotopic labelled proteins?
18. How a small molecular structure can be refined and
explain all the parameters those should be considered
during refinement?
19. Narrate the structure biology applications towards drug
designing.
20. Explain the role of torsion angle concept in structure
prediction and validation of protein structure.


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  • biomolecules
  • computational approach to taxonomy and phylogeny
  • computational biology
  • elective i –– general chemistry
  • elective ii — immunology and immunotechnology
  • genomics and pharmacogenomics
  • introduction to bioinformatics
  • lab ii : biochemical and molecular biology methods
  • lab iii – mysql and perl programming
  • mathematics and biostatistics
  • molecular cell biology and genetics
  • molecular modelling and pharmacoinformatics
  • nanotechnology and advanced drug delivery system
  • principles of gene manipulation
  • structural biology