Universal Science College

(B. Sc. Biochemistry)

Second Semester 2005
Internal Examination Full Marks: 100
Subject: Biochem 125 ( Biomolecules I) Pass Marks: 45
Date: July 30, 2005 Time: 3 hours
Candidates are required to give their answers in their own words as far as practicable. The
figure in the margin indicates full marks.
Group (A) Long Questions (Any three) ×14 = 42)
(3×

1. Explain the structures of typical peptidoglycan, glycosoaminoglycan, proteoglycan and

glycolipid.
2. Describe strategies for amino acid sequencing of a protein.
3. Describe the principle and application of size exclusion chromatography.
4. What are the levels of protein structure? Discuss in detail secondary structure of protein.

Group (B) Short Questions: (Any six) ×7 = 42)

(6×
1. Explain briefly the principle of carbohydrate analysis.
2. Explain glycoproteins as information rich proteion.
3. What would be the overall yield of a peptide containing 10 aminoacid residues if the yield for
incorporation of each were 70%.?
4. Describe chemical synthesis of peptides.
5. Describe isoelectric focusing of proteins
6. Point out the mechanism of ion exchange chromatography .
7. Describe denaturation and renaturation of protein.
8. What are the factors that affect - helix stability? Explain.

Group (C) Write short notes on: (Any eight) ×8 = 16)

(2×

1. What are integrins?

2. What are ganglosides?
3. What is the function of glycogen?
4. Write short note on two dimensional electrophoresis?
5. Why the bands in SDS PAGE is observed as bow shaped?
6. Write in brief about hydrophobic chromatography.
7. How is the N-terminal of amino acid determined?
8. What is the principle behind the purification of protein by salt?
9. What are proteins?
10. What are supramolecular complexes?
11. Give brief account on Ramachandran plot.
12. The peptide bond is rigid and planar. Why?
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