Page 132 - handbook 20162017
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Faculty of Science Handbook, Session 2016/2017
SIJ 2004 METABOLISM AND REGULATION OF AMINO Medium of Instruction:
ACIDS AND NUCLEIC ACIDS English
The objectives and content of the course are designed to Soft Skills:
provide students with a comprehensive understanding of CT2, CS3, LL2
the metabolic pathways involving the amino acids and
nucleotides; and the manner by which metabolism is Main References:
regulated. This course stresses both the normal metabolic 1. Berg, J.M., Tymoczko, J.L., Stryer, L. & Gatto, Jr., G.J.
th
function, and why disease states occur if normal metabolic (2012) Biochemistry, 7 ed., W.H. Freeman: New York
th
processes are disrupted. 2. Voet D. & Voet J.G. (2011) Biochemistry, 4 ed., John
Wiley: New York
Assessment Methods: 3. Mathews C.K., van Holde K.E., Appling, D.R. &
th
Continuous Assessment: 40% Anthony-Cahill, S.J. (2013) Biochemistry, 4 ed.,
Final Examination: 60% Pearson: Ontario
4. Nelson, D.L. & Cox M.M. (2013) Lehninger Principles
th
Medium of Instruction: of Biochemistry, 6 ed., W.H. Freeman: New York
English 5. Tayyab S. & Boyce A.N. (2006) A Journey from Amino
Acids to Proteins, University Malaya Press: Kuala
Soft Skills: Lumpur
CS3, CT3, LL2
Main References: SIJ 2007 ENZYMES: MECHANISM AND CONTROL
1. Nelson, D.L. and Cox, M.M., W.H. (2013) Lehninger:
Principles of Biochemistry 6th ed., Freeman and Enzymes as catalysts - Activation energy and biocatalysis;
Company (New York). Enzyme specificity; Enzyme kinetics - Effect of enzyme
2. Devlin, T.M (2011). Textbook of Biochemistry with concentration, substrate concentration, pH and
Clinical Correlations 7th ed.John Wiley & Sons, Inc. temperature on reaction velocity; Michaelis-Menten
(New York). equation and linear transformations; Enzyme inhibitions -
Competitive, Noncompetitive, Uncompetitive and
Irreversible inhibitions; Active site mapping and
SIJ 2005 MOLECULAR BIOLOGY intermediate detection; Enzyme mechanisms with special
reference to lysozyme and chymotrypsin; Enzyme
This course explains the biosynthesis of Nucleic Acid, regulation - Zymogen activation, Covalent modification,
DNA and RNA. Replication process, trancription and Physiological control and Allosteric regulation; Bi-
translation are also explained in detail. This course also substrate reactions; Catalytic antibodies; Ribozymes
covers mutation and how the cells carry out DNA repair;
various genetic process such gene recombination anf Assessment Methods:
transposition; chromosamal inheritance versus Continuous Assessment : 40%
ectrachromosamal inheritance. Final Examination : 60%
Assessment Methods: Medium of Instruction:
Continuous Assessment: 40% English
Final Examination: 60%
Soft Skills:
Medium of Instruction: CT3, CS3, LL2
English
Main References:
1. Berg, J.M., Tymoczko, J.L., Stryer, L. & Gatto, Jr., G.J.
Soft Skills: (2012) Biochemistry, 7 ed., W.H. Freeman: New York
th
th
CT3, LL2 2. Voet D. & Voet J.G. (2011) Biochemistry, 4 ed., John
Wiley: New York
Main References: 3. Mathews C.K., van Holde K.E., Appling, D.R. &
th
th
1. Snustad. (2012) Principles of genetics. 7 Edition Anthony-Cahill, S.J. (2013) Biochemistry, 4 ed.,
John Wiley Pearson: Ontario
2. Devlin. (2013) Textbook of biochemistry. John Wiley 4. Price N.C. & Stevens, L. (1999) Fundamentals of
3. Stryer. (2012) Biochemistry. Freeman Enzymology, 3 ed. Oxford University Press
rd
4. Watson. (2012) Molecular biology of the gene.
Pearson/Benjamin Cummings
5. Lewin. (2012) Genes VIII. Oxford University Press. SIJ 2008 BIOCHEMISTRY PRACTICAL I
This practical course introduces the students with
SIJ 2006 PROTEIN BIOCHEMISTRY fundamental techniques in the field of biochemistry. Apart
from that the students also will learn the methods of
Levels of protein structures - Primary structure, its scientific calculation and report writing. Among the
importance and its determination; Secondary structures biochemical techniques the students will learn are
and their prediction; Super- secondary structures; Tertiary fundamental practice in buffer solution preparation,
structure and forces involved in its stabilization; spectrophotometer usage in biochemical experiments,
Quaternary structure; Protein folding and denaturation; isolation and purification of biomolecules and enzyme
Protein engineering; Protein purification and kinetics.
characterization.
Assessment Methods:
Assessment Methods: Continuous Assessment: 100%
Continuous Assessment: 40%
Final Examination: 60%
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