SREE SASTHA INSTITUTE OF ENGINEERING AND TECHNOLOGY
BT 6501-PROTEOMICS AND PROTEIN STRUCTURE AND FUNCTION
PART-A
1. Write the structure of a tripeptide in which glycine is one of the amino acid.
2. Define isoelectric point of a protein.
3. Differentiate primary from secondary structure of proteins.
4. What are the contributions of Fred Sanger in protein chemistry?
5. Write a note on structural features of the peptide bond
6. Comment on “Loop regions appear always at the surface of a protein”.
7. What are the functions of Cro protein and repressor proteins in gene expression?
8. Classify proteases based on their amino acids at their active site
9. List out the methods by which a protein can be engineered to enhance its properties.
10. Name any two proteins used for diagnostics and therapeutics.
11. What is the importance of tertiary structure in proteins?
12. Define post translational modification?
13. What are the methods of predicting 3D structure of proteins?
14. What is protein-protein interaction?
15. Define coordinate & hydrophobic bonds?
16. Differentiate between covalent & Ionic bonds?
17. What is Trp repressor?
18. What is helix turn helix in DNA binding?
19. What are membrane proteins?
20. How do you predict the secondary structure of proteins?
21. What is protein folding and its importance.
PART-B
1. a) (i) Write the steps involved in 2D gel electrophoresis techniques to characterize a
protein in terms of its isoelectric point and molecular weight.
(ii) Write a Ramachandran plot of a protein.
2. b) (i) How would disulfide bonds contribute to the protein’s stability?
(ii) Discuss in detail on the role of different non-covalent interactions in protein structure
and function.
3. a) (i) Write in detail on high through-put protein sequencing using MALDI-T0f MS.
b) (i) Write a brief note on nucleotide binding proteins.
(ii) How glycine and proline have an opposite effects on protein stability.
4. a) (i) Discuss in detail on protein folding with suitable examples.
(ii) What is the fate of protein if it is misfolded?
b) How is X-ray diffraction techniques used to determine the 3D structure of proteins and a
note on its limitations.
5. a) (i) Write a note on the formation of antigen-binding site in immunoglobulins.
(ii) Elaborate on the role of eukaryotic transcription factors in gene expression.
b) (i) What are the structural features required for the catalytic action of proteases?
(ii) Write a note on formation of tetrahedral intermediates during protease active proteins.
6. a) (i) Discuss any TWO methods of protein engineering with underlying principles.
(ii) Write a note on engineered lysozymes for specific applications
b) Write a note on the following (i) Abzymes (ii) HIV proteases
7. Explain in detail about mass spectrometry and prediction of 3D structure of protein
8. Explain about X-ray crystallography in structure prediction of proteins.
9. Describe about Chemical reactivity in relation to post-translational modification
10.Explain about Edman degradation method & peptide sequencing in detail.
11. Explain the different components of proteomics?
12. Describe in detail on yeast hybrid system.