Q.4: a). what are G proteins? How are G proteins activated and inactivated?

Q.5: a).What are intracellular events following the activation of Gq proteins? 2

Q.23: Classify amino acids on the basis of their side chains (R groups). What are standard and non
standard amino acids? 3, 1.

Q.24: what is the role of amino acid side chain (R group) in protein folding? Briefly describe the
relationship of protein structure to its functions. Give at least one example. 2

Q.25: a). What is selenocsteine? Write down its significance. 1.5

Q.25:a). Define Secondary structure of proteins. Differentiate between alpha α helix and beta β pleated
sheets.

Q.26: a). what is the role of amino acid side chain (R group) in protein folding? Briefly describe the
relationship o protein structure to its functions. Give at least one example. 2

Q.27: a).name different types of secondary structure present in proteins. Explain any two of them. 0.5, 2

Q.28: a). what are simple proteins? 2

B). Give structural and chemical characteristics of collagen. 2

B).How secondary structure of proteins is formed? 2

Q: 48. A). Name the hemoproteins along with their principal biological functions. 2

Q: 50. Compare the properties of hemoglobin and myoglobin. Also draw oxygen dissociation curves of
hemoglobin and myoglobin. 3+1

Q.57: a). Name the hemoproteins along with their principal biological functions. 2

Q.58: a). What is calcitriol? How it is formed in body? 1, 1

B). Give biochemical changes in rickets. 2

Q.64: a). Why does gamma carboxylation of glutamate residues of clotting proteins of vitamin K lead to
platelet aggregation? 1.5
Iv). What is the biochemical defect undergoing neuropathy? 0.5

Q.66: HOW VITAMIN D id synthesized and activated in the body? Name the diseases that occur due to
its deficiency. 2, 2.

Q.69: a). Define the terms: 2

Body mass index