Proteins And Protein Metabolism Set 3

1. In proteins the α-helix and β-pleated sheet
are examples of

2. Globular proteins have completely folded,
coiled polypeptide chain and the axial
ratio (ratio of length to breadth) is

3. The lipoprotein with the fastest electrophoretic mobility and the lowest triglyceride content is

4. The apolipoprotein which acts as ligand
for LDL receptor is

5. The apolipoprotein which from the
integral component of VLDL is

6. Each turn of α-helix contains the amino
acid residues (number):

7. At the lowest energy level α-helix of
polypeptide chain is stabilised

8. The apolipoprotein which forms the
integral component of chylomicron is

9. The apolipoprotein which acts as activator
of extrahepatic lipoprotein is

10. The primary structure of fibroin, the
principal protein of silk worm fibres
consists almost entirely of

11. The a-helix of proteins is

12. Along the α-helix each amino acid residue
advances in nm by

13. Denaturation of proteins results in

14. Tertiary structure of a protein describes

15. the number of helices present in a
collagen molecule is

16. Serum LDL has been found to be increased
in

17. The hydrogen bonds between peptide
linkages of a protein molecules are interfered by

18. In a protein molecule the disulphide bond
is not broken by

19. Distance traveled per turn of α−helix in
nm is

20. The technique for purification of proteins
that can be made specific for a given
protein is

21. Fibrous proteins have axial ratio

22. The lipoprotein associated with activation
of LCAT is

23. Both α-helix and β-pleated sheet conformation of proteins were proposed by

24. Ceruloplasmin is

25. The apolipoprotein which acts as activator
of LCAT is