Page 82 - buku panduan 20192020

Faculty of Science Handbook, Session 2019/2020

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
Medium of Instruction: of Biochemistry, 6 ed., W.H. Freeman: New York
th
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:
Soft Skills: 1. Berg, J.M., Tymoczko, J.L., Stryer, L. & Gatto, Jr., G.J.
th
CT3, LL2 (2012) Biochemistry, 7 ed., W.H. Freeman: New York
2. Voet D. & Voet J.G. (2011) Biochemistry, 4 ed., John
th
Main References: Wiley: New York
th
1. Snustad. (2012) Principles of genetics. 7 Edition 3. Mathews C.K., van Holde K.E., Appling, D.R. &
th
John Wiley Anthony-Cahill, S.J. (2013) Biochemistry, 4 ed.,
2. Devlin. (2013) Textbook of biochemistry. John Wiley Pearson: Ontario
3. Stryer. (2012) Biochemistry. Freeman 4. Price N.C. & Stevens, L. (1999) Fundamentals of
rd
4. Watson. (2012) Molecular biology of the gene. Enzymology, 3 ed. Oxford University Press
Pearson/Benjamin Cummings
5. Lewin. (2012) Genes VIII. Oxford University Press.
SIJ 2008 BIOCHEMISTRY PRACTICAL I

SIJ 2006 PROTEIN BIOCHEMISTRY This practical course introduces the students with
fundamental techniques in the field of biochemistry. Apart
Levels of protein structures - Primary structure, its from that the students also will learn the methods of
importance and its determination; Secondary structures scientific calculation and report writing. Among the
and their prediction; Super- secondary structures; Tertiary biochemical techniques the students will learn are
structure and forces involved in its stabilization; fundamental practice in buffer solution preparation,
Quaternary structure; Protein folding and denaturation; spectrophotometer usage in biochemical experiments,
Protein engineering; Protein purification and isolation and purification of biomolecules and enzyme
characterization. kinetics.

Assessment Methods: Assessment Methods:
Continuous Assessment: 40% Continuous Assessment: 100%
Final Examination: 60%

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