Structural Biochemistry 1 (BCHS3101)
BSc, Chemistry - CHMS
Semester: First Semester
Level: 300
Year: 2017
REPUBLIC OF CAMEROON THE UNIVERSITY OF BAMENDA
Peace-Work-Fatherland
P. O. BOX 39 Bambili
School/Faculty:Science Department:_Biochemistry Lecturer(s): Dr Nantia & Pr
Mbouobda____
Course Code: _BCHS3101_______ Course Title: Structural Biochemistry I__
Date: _18-09-2017_______Halls: __Asanji ________Time: 15:00-17:00__
Instructions: ___Answer questions in ordering manner and do not miss different exercises.
Exercise 1 (24 marks)
a) Structure of and function of β-alanine, homoserine, glutathion (3.5 mrks)
b) The peptides following are subjected to normal electrophoretic analysis at pH 5.0. (i) GR (ii) FRS (iii) EPA
(iv) VYE
i) Give the structure and systematic name of the peptides (3 mrks)
ii) Illustrate the changes susceptible occur on the peptides in increasingly acidic medium (4
mrks)
iii) Predict the relative rate of migration of each peptide in the electrophoretic field (3 mrks).
c) Fill the table with the effects and justifications of the following treatments on the peptide
TAKE (10.5 mrks):
Treatment Effect Justification
l)Trypsin
2) Saturated AgNO
3
3) Boiling
4) UV radiation
5) DNFB
6) 6M HC1
7) Saturated (NH
4
)
2
SO
4
solution
Exercise 2 (11 marks)
1) In a table compare (structure, Systematic name, class) of deoxythymidylate and guanylate (3 mrks).
3) Give the structure and the biological function of S-adenosylmethionine (SAM) (3 mrks)
4) Give the principle of the Sanger sequencing method in nucleic acid analysis (2 mrks)
5) Harmful and deadly snakes are because of the poisonous venom they possess. Research has shown that the
deadly potential of the venom may involve its action on the genetic material of the bitten individual. Justify
this assertion using your knowledge in Biochemistry (3 mrks).
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