Exam Details
Subject | small and macromolecular x-ray crystallography | |
Paper | ||
Exam / Course | p.g. diploma in structural pharmacogenomics bioinformatics | |
Department | ||
Organization | alagappa university | |
Position | ||
Exam Date | December, 2017 | |
City, State | tamil nadu, karaikudi |
Question Paper
P.G. DIPLOMA IN STRUCTURAL
PHARMACOGENOMICS EXAMINATION,
DECEMBER 2017
First Semester
Bioinformatics
SMALL AND MACROMOLECULAR X-RAY
CRYSTALLOGRAPHY
(CBCS 2013 onwards)
Time 3 Hours Maximum 75 Marks
Part A (10 x 2 20)
Answer all the questions.
1. State Bragg's law.
2. Define Diffraction.
3. Name the techniques used for crystal growth.
4. State the principle of X-Ray crystallography.
5. Write any two advantages of Co-Crystallization.
6. What is electron density?
7. What are electrostatic interactions?
8. Name the bonds seen in Protein DNA interactions.
9. What is structural genomics?
10. State the role of structure validation.
Sub. Code
510103
RW-1392
2
Sp 5
Part B x 5 25)
Answer all questions.
11. Explain briefly about X-Ray diffraction pattern.
Or
Write about Bravais lattices and crystal systems.
12. Describe about single crystal X-Ray data collection.
Or
Discuss the methods used in the refinement of
crystal structure.
13. Write about electron density maps.
Or
Explain the methods used in structure refinement.
14. Explain briefly about protein-protein interaction.
Or
Explain briefly about DNA-small molecule
interaction
15. Describe about protein-DNA interaction.
Or
Discuss about nucleic acid structure determination.
RW-1392
3
Sp 5
Part C x 10 30)
Answer any three questions.
16. Explain in detail about electron density calculations and
its role in crystallography.
17. Describe in detail about various techniques used in
crystal growth.
18. Explain Fourier synthesis and least square techniques.
19. Explain in detail about NMR.
20. Explain in detail about any three protein structure
determination methods.
——————
PHARMACOGENOMICS EXAMINATION,
DECEMBER 2017
First Semester
Bioinformatics
SMALL AND MACROMOLECULAR X-RAY
CRYSTALLOGRAPHY
(CBCS 2013 onwards)
Time 3 Hours Maximum 75 Marks
Part A (10 x 2 20)
Answer all the questions.
1. State Bragg's law.
2. Define Diffraction.
3. Name the techniques used for crystal growth.
4. State the principle of X-Ray crystallography.
5. Write any two advantages of Co-Crystallization.
6. What is electron density?
7. What are electrostatic interactions?
8. Name the bonds seen in Protein DNA interactions.
9. What is structural genomics?
10. State the role of structure validation.
Sub. Code
510103
RW-1392
2
Sp 5
Part B x 5 25)
Answer all questions.
11. Explain briefly about X-Ray diffraction pattern.
Or
Write about Bravais lattices and crystal systems.
12. Describe about single crystal X-Ray data collection.
Or
Discuss the methods used in the refinement of
crystal structure.
13. Write about electron density maps.
Or
Explain the methods used in structure refinement.
14. Explain briefly about protein-protein interaction.
Or
Explain briefly about DNA-small molecule
interaction
15. Describe about protein-DNA interaction.
Or
Discuss about nucleic acid structure determination.
RW-1392
3
Sp 5
Part C x 10 30)
Answer any three questions.
16. Explain in detail about electron density calculations and
its role in crystallography.
17. Describe in detail about various techniques used in
crystal growth.
18. Explain Fourier synthesis and least square techniques.
19. Explain in detail about NMR.
20. Explain in detail about any three protein structure
determination methods.
——————
Other Question Papers
Subjects
- elective – i — immunoinformatics
- lab i : computer aided drug designing (theory)
- lab ii : structural biology (theory)
- molecular cell biology and genetic engineering
- molecular modeling and drug designing
- pharmacogenomics
- small and macromolecular x-ray crystallography