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1-      Haemoglobin and collagen are proteins with diverse functions. Describe how the structures of proteins can be correlated with their functions.

2-      Define protein denaturation. Explain why, when insulin or majority proteins are subjected to denaturation and renaturation conditions, they regain only a few percent of their original activities.

3-      What is the basis of the classification of amino acids? Give one example for each class of amino acids.

4-      What is protein denaturation? Explain the significance of the denaturation-renaturation experiments on ribonuclease.

5-      What are the salient features of an alpha helix? Name the amino acids that destabilize this structure.

6-      Name two modified amino acids found in proteins and state their biological functions.

7-      Discuss fully the primary, secondary, tertiary and quaternary structure of proteins. Illustrate your answer with suitable example

8-      Distinguish between a simple and a conjugated protein. Illustrate your answer with suitable examples.

9-      What are the buffering groups present in a protein at physiological pH? Show how these groups help to contribute to buffering capacity.

10-   Draw the structure of any ammo acids as: (i) zwitterion (ii) cationic form (iii) anionic form

11-   Draw the structure of a dipeptide. Use R to represent the side chain of an amino acid.

12-   Describe the special roles of glycine and proline in protein structure.

13-   What is the stereochemical difference between D-alanine and L-alanine?

14-   What are the main characteristics of globular and fibrous proteins? Give an example of each of these proteins.

15-   Explain how a proline residue in polypeptide chain interrupts the alpha-helical structure.

16-   What are standard or primary amino acids? Give examples of non standard amino acids.

17-   What is iso electric p H ? What are the commercial applications of iso electric p H?

18-   Justify the statement, “Primary structure guides the formation of secondary and tertiary structure”, give example in support of your answer.

19-   What is protein misfolding? Give examples and discuss the clinical significance of protein misfolding.

20-   How is a peptide bond formed between the two amino acids? Discuss the characteristics of a peptide bond.

21-   Enlist the biologically important peptides; Give a brief account of the functions of Glutathione.

22-   Enlist the important functions of amino acids.

23-   What are the various ways by which proteins can be classified? Give examples of each category of proteins.

24-   Compare and contrast the structural features of α helix and β pleated sheets. Give examples of proteins having predominance of these structures.

25-   What is a domain? How is it formed, what kind of forces stabilize its structure?

26-   Give an account of the properties of amino acids, state the clinical significance if any of such reactions.

27-   An 80- year-old male was brought for consultation to  a Medical OPD with the chief complaints of loss of memory and disorientation from the past few months. He was diagnosed with Alzheimer disease. Discuss the biochemical basis, clinical symptoms and the prognosis of this disease.

28-   “Primary structure is guided by information on DNA. A single nucleotide change on DNA can alter the information and thus the sequence of amino acids in a peptide chain with the resultant loss of partial or total functional capacity of the protein”. Comment on the statement.

29-   Enlist the names of the tests performed for detection of specific amino acids in a sample.

30-   Give a brief account of the agents which can bring about protein unfolding? Discuss the biological or clinical aspect of protein denaturation.

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