Saturday 22 March 2008

JNU MSc BIOTECHNOLOGY




CENTRE FOR BIOTECHNOLOGY
JAWAHARLAL NEHRU UNIVERSITY

SYLLABUS FOR MSc BIOTECHNOLOGY

Ist SEMESTER

COURSE NO.- TITLE OF COURSE - CREDITS

BT 511 - Mathematics for Biologists - 3
BT 512 - Biophysical Chemistry - 3
BT 513 - Computational Biology I - 2
BT 514 - Biochemistry - 3
BT 515 - Enzymology - 2
BT 516 - Immunology - 2
BT 517 - Cell Biology - 2
BT 518 - Laboratory Techniques I - 4

Total 21

2nd SEMESTER

BT 521 - Molecular Biology and Molecular Genetics - 5
BT 522 - Bioprocess Technology - 3
BT 523 - Engineering Principle - 2
BT 524 - Laboratory TechniquesII - 4
BT 525 - Term Paper - 1
One non credit course from any School of the University No credit

Total 15

3rd SEMESTER

BT 531 - Computational BiologyII - 3
BT 532 - Molecular Biology of Eukaryotic Systems - 2
BT 533 - Genetic Engineering - 3
BT 534 - Immunotechnology - 2
BT 535 - Journal Clubs I - 1
BT 536 - Project - 5
Any one optional course of 2 credit from SLS as per students interest 2

Total 18

4th SEMESTER

BT 541 - Journal ClubII - 1
BT 542 - Project - 9
BT 543 - Project Presentation - 3*

Total 13

Total

Ist 21
2 nd 15 + Non credit course
3 rd 18 (INCLUDING 2 CREDIT OPTIONAL COURSE FROM SLS)
4 th 13

All Total 67**

Credit raised to 3 (FROM 2) vide SCM Mts dated 9 th March 2005, Item No.7
** Minimum credits required for award of MSc degree is 64

Course No.BT 511 - Mathematics for Biologists - Credits: 2

Preliminaries: Coordinates, lines and increments, function, shifting graphs, trigonometric
functions.

Limits and Continuity: Rates of change and limits, rules for finding limits, target values and
formal definitions of limits, extensions of the limit concept, continuity, tangent lines.

Derivatives: The derivative of a function, differentiation rules, rates of change, derivatives of
trigonometric functions, the chain rule, implicit differentiation and rational exponents, related
rates of change.

Applications of derivatives: Extreme values of functions, the mean value theorem, the first
derivative test for local extreme values, graphing with y’ and y”,, limits as x→ ±∞, Asymptotes,
and dominant terms, optimization, linearization and differentials, Newton’ method.
Integration: Indefinite integrals, differential equations, initial value problems and mathematical
modeling, integration by substitution running the chain rule backward, estimating with finite
sums, Riemann sums and definite integrals, properties, area and the mean value theorem, the
fundamental theorem, substitution in definite integrals, numerical integration.

Applications of integrals: Areas between curves, finding volumes by slicing, volumes of solids
of revolution disks and washers, cylindrical shells, lengths of plane curves, areas of surfaces of
revolution, moments and centres of mass, work, fluid pressures and forces, the basic pattern and other modeling applications.

Course No. BT 512 - Biophysical Chemistry Credits: 3
BIOPHYSICAL CHEMISTRY

COURSE NO. : BT 512 CREDITS : 3
Lectures =
A. Interactions in Biological Systems
1. Intra and inter molecular forces electrostatic interactions and Hydrogen
bonding interactions = 1
2. van der Waals and Hydrophobic interactions = 1
3. Disulphide bridges = 1
4. Role of water and weak interactions = 2
B. Structure of Proteins
1. Conformational properties of polypeptides = 1
2. Primary and secondary structure = 2
αhelix, βsheet structures etc.
3. Tertiary and quarternary structure = 2
4. Structural features of membrane proteins = 2
5. Secondary and tertiary structure prediction of protein conformation = 2

C. Multiple equilibrium
1. Titration of proteins to evaluate net and total charge = 2
2. Scatchard and Hill plots = 2

3. Folding unfolding equilbrium and denaturation of proteins = 2
4. Effect of temperature and solvent conditions on the thermodynamics of protein folding unfolding equilibrium = 2
5. Kinetics of protein folding = 2

D. Techniques for the study of Macromolecular Structure
1. Analytical Ultracentrifugation : Sedimentation velocity and equilibrium, determination of molecular weights = 2
2. Micro calorimetry (DSC and ITC) and its application = 2
3. Circular Dichroism spectroscopy = 2
4. UV, visible and Fluorescence spectroscopy = 3
5. Xray Diffraction = 3
6. Nuclear Magnetic Resonance (NMR) = 3
8. Mass Spectrometry = 2

TOTAL LECTURES 41
Reading Material
1. Proteins: Structure and Molecular Properties by T.E. Creighton
2. Biophysical Chemistry Part I & II by C.R. Cantor and P.R. Schimmel
3. Physical Biochemistry by K.E. van Holde
4. Physical Biochemistry by David Freifelder
5. Introduction to Protein Structure: C. Branden and J. Tooze
6. Protein Physics by A.V. Finkelstein and O.B. Ptitsyn

Course No.BT 513 Computational BiologyI Credits: 2
Biological Sequence Databases:
Overview of various primary and secondary databases that deal with protein and nucleic
acid sequences. Databases to be covered in detail are GenBank, EMBL, DDBJ, SwissProt, PIR,
and MIPS for primary sequences. Various specialized databases like TIGR, Hovergen, TAIR,
PlasmoDB, ECDC etc., will also be discussed. Preliminary ideas of query and analysis of
sequence information.
Sequence Comparison Methods:
Method for the comparison of two sequences viz., Dot matrix plots, NeedlemanWusch
& Smith Waterman algorithms. Analysis of computational complexities and the relative merits
and demerits of each method. Theory of scoring matrices and their use for sequence comparison.
Database Search Algorithms:
Methods for searching sequence databases like FASTA and BLAST algorithms.
Statistical analysis and evaluation of BLAST results.
Pattern Recognition Methods in Sequence Analysis:
Concept of a sequence pattern, regular expression based patterns. The use of pattern
databases like PROSITE and PRINTS. Concept of position specific weight matrices and their
use in sequence analysis. Theory of profiles and their use with special reference to PSIBLAst.
Markov chains and Markov models and their use in gene finding. Concept of HMMS, the
forwardbackward and the Viterbi algorithm. The BaumWelch algorithm for training a HMM.
Use of profile HMM for protein family classification.

Course No.BT 514 Biochemistry Credits: 3
Lectures =
1. Biochemistry : The molecular logic of living organisms = 1
2. The cell and its biochemical organization = 2
3. Metabolism: Basic concept and design = 2
4. Glycolysis: Key structure and reactions, formation of 1,6 bisphosphate, formation of glyceraldehyde 3phosphate, formation of pyruvate and generation of second ATP, entry
of fructose and galactose into glycolysis, phosphofructokinase as key enzyme in glycolysis,
hoxokinase and pyruvate kinase as regulatory enzymes, conversion of pyruvate into ethanol lactate or acetyl CoA. = 3
5. Pentose phosphate pathway : Generation of NADPH and interconnection of glycolysis and pentosephosphate pathway, control of rate of pentose phosphate pathway by
NADPH+, regulation of flow of glucose 6 phosphate by the need of NADPH, ribose 5 phosphate and ATP, glucose 6 phosphate dehydrogenase defficiency. = 2
6. Gluconeogenesis: Synthesis of carbohydrates by noncarbohydrate precursors, gluconeogenes is not a reversal of glycolysis, activation of pyruvate carboxylase by acetyl CoA, oxaloacetate shuttle, energy consumption in the synthesis of glucose from pyruvate, reciprocal regulation of gluconeogenesis and glycolysis, conversion of lactate and alanine into glucose in liver. = 2
7. Citric acid cycle: Formation of acetyl CoA from pyruvate, condensation of oxaloacetate with acetyl CoA to form citrate, isomerization of citrate into isocitrate, oxidative decarboxylation of succinyl CoA, generation of high energy phosphate from succinyl CoA, regeneration of oxalate, sloichiometry of citric acid cycle, pyruvate dehydrogenase complex, citric acid cycle as a source of biosynthetic precursors, control of pyruvate dehydrogenase complex, control
of citric acid cycle, citric acid cycle and its high energy yield. = 3
8. Electron transport and oxidative phospherylation, energetics of oxidative phosphorylation, en enrgy yield by complete oxidation of glucose. =3
9. Amino acid degradation oxidative deemination, conversion of NH4+ into urea, linkage between urea cycle and citirc acid cycle, conversion of alanine serine and cystein into pyruvate, conversion of aspartate and asparagine into oxalocetate, conversion of several amino acid into alpha ketoglutarate through glutamate, succinyl CoA as a point of entry for some amino acids, leucine degradation to acetyl CoA and acetoacetyl CoA, phenyl alanine degradation to acetoacetate and fumarate. = 3
10. Biosynthesis of amino acids : Conversion of nitrogen to NH4 by microorganisms, conversion of amonia into amino acids by way of glutamata and glutamine, conversion of citric acid Intermediates to amino acids, glutamate as precursor of glutamine, proline and
arginine, conversion of 3phosphoglycerate to serine, synthesis of cystein from serine and homocysteine, feed back regulation of amino acid biosynthesis. = 3
11. Biosynthesis and degradation of Nucleotides: Purine biosynthesis : formation of PRPP, Biosynthesis of IMP, Purine nucleotide interconversions, regulation of purine
biosynthesis. = 2
Pyrimidine Biosynthesis : Assembly of the pyrimidine nucleus, synthesis of di & tri phosphates, formation of deoxyribonucleotides, thymine biosynthesis salvage pathway for purine and pyrimidine nucleotides, Degradation of purines and pyrimidines to uric acid and urea. = 3
12. Lipids : Fatty acids, glycerols, waxes, phospholipids, sphingolipids, sterols lipoproteins = 3
13. Fatty acid oxidation Digestion, mobilization and transport of fatty acids,
Mobilization of stored triglycerides by hormones, activation of fatty acids and their transport to
mitochondria, oxidation of saturated fatty acids, Oxidation of unsaturated fatty acids, and oxidation of odd chain fatty acids. Ketone bodies, over production of kelone bodies. = 3
14. Biosynthesis of fatty acids Formation of malony CoA, fattyacid synthase complex, fatty
acid synthase multifunctional proteins, shuttling of acitate out of mitochondria as citrate, Reactions of fatty acid synthase, regulation of fatty acid biosynthesis, Biosynthesis
of triglycerols, membrane phospholipids and prostaglandins. = 3
15. Integration of Metabolism = 1
TOTAL LECTURES = 36

Course No.BT 515 Enzymology Credits: 2
Lectures =
1. Enzymes
General characteristics and Catalytic power of enzymes and their classification = 1
Energy considerations = 1
Factors affecting enzyme activity = 1
Enzyme kinetics, Michaelis Menten equation = 1
Allosteric enzymes and their regulation = 1
Enzyme inhibition, activation of enzymes = 1
Immobilized enzymes = 1
Different mechanisms of enzyme catalysis acidbase and covalent catalysis = 3
Molecular mechanism of action of chymotrypsin = 1
Lysozyme and carboxy peptidase = 1
Structure function relationship of enzymes = 1
2. Biological membranes : Structure, function and dynamics = 2
3. Transport of biomolecules into the cells = 2
4. Signal Transduction cascades, Receptor higgerd phosphorylation cascade, G protein
cascade, cyclic CAMP as a second messenger, protein kinases, receptor higgard hydrolysis of phosphotidyl inositol, IP3, Diacyl glycerol, calcium ion as a cytosolic messenger,
Calmodulin = 3

5. Secondary metabolites with special reference to antibiotics and microbial toxins = 2+2
TOTAL LECTURES = 24
Course No. BT 516 Immunology Credits: 2
A. The Immune System 3 lectures
1. Innate Immune response and its role in protection
2. Adaptive Immune response

The humoral and cellular component of the Immune response, Overlap between Innate and adaptive immunity.
3. Cells involved in the Immune response

The lymphoid organs, their interaction
B. The antigens seen by the Immune System 3 lectures
1. Antigenicity and Immunogenicity
2. The epitopes seen by B Cells and T Cells
3. Antigen engineeringIncreasing
Immunogenicity
C. Antibody Molecule 5 lectures
1. Structure of antibody molecules
2. Function of antibody molecules
3. AntibodyAntigen interactions
4. Generation of antibody diversity
5. Antibody engineering Hybridoma secreting monoclonal antibodies
Recombinant antibody molecules
D. Major Histocompatibility Complex 2 lectures
1. MHC molecules and organisation of their genes
2. Structure and function of MHC gene products
E. Antigen Presentation 2 lectures
1. Antigen processing
2. Role of MHC and nonMHC molecules
In antigen presentation
F. T Cell receptor 5 lectures
1. ab T cells
2. gd T cells
3. TCRCD complex
4. Structure of TCR and its interaction With MHCI and MHCII peptide Complex T
cell selection
5. Organization of TCR gene segments And their rearrangement

G. Activation of T cells 3 lectures
1. Activation TH and TC cells
2. Generation of T memory cells
3. Apoptosis in T cells
H. B Cell matuvation 2 lectures
1. Activation of B Cells
2. Regulation of B Cell mediated Effector functions
I. Cytokines 3 lectures
1. Structure of Cytokines
2. Cytokine receptors
3. Function of Cytokines
J. The Complement System 2 lectures

K. Cell mediated effector responses 2 lectures

Course No.BT 517 Cell Biology Credits: 2

Lectures =
A. Plasma membrane : Composition and structure : = 2
Membrane associated receptors. Artificial membranes
(liposomes)
B. Membrane proteins and principles of membrane
Organization. Cell junction. = 1
C. Cytoskeleton : topography, Microtubules, microfilaments,
lattice and cytosol =2
D. Microtubules and cell mobilitycilia and flagella = 1
E. Cell organelles and secretion : Golgi, endoplasmic reticulum, lysosomes, peroxisomes. Internalization of macromolecules and particles : endo and exocytosis. = 1
F. Mittochondrial structure and oxidative phosphorylation = 1
G. Nucleus : Nuclear envelope, nucleolus, chromosomes = 1
H. Cell division and cell cycle : Go G1 transition. = 2
Chromosome movements Regulation of cell division.
I. Cell differentiation : cortical differentiation, Nuclear
differentiation, differentiation of erythrocytes. Difference between normal and cancer cells. =1

Course No.BT 518 Laboratory TechniquesI
Credits: 4
General
a. Making of buffers
b. Titration of Polybasic acids and evaluation of pKa’s
c. Titration of amino acids
d. Two dimensional TLC of amino acids
e. Paper chromatography of carbohydrates
Proteins :
a. Isolation of proteins
b. Estimation of proteins by Lowry and Brandford methods
c. Gel filtration, ionexchange
and affinity chromatography
d. Gel Electrophoresis
e. Wavelength scan of proteins
f. Thermal unfolding of proteins and calculations of thermodynamic parameters
from temperature scanning UV spectrophotometer, Effect of solvent conditions
on thermal stability of proteins.
g. pH titrations of protein, calculation of net charge and total charge at a particular pH.
h. Reduction of disulphide bonds of proteins.
DNA and RNA
a. Isolation of DNA and RNA
b. Estimation of DNA and RNA by chemical means
c. Wavelength scan of DNA and RNA
d. Melting studies of calf thymus DNA
Carbohydrates:
a. Estimation of glucose by Glucose oxidase (Trinder’s reagent)
b. Estimation of reducing sugars by Nelson Somogyi’s method
c. Effect of temperature, time and substrate concentration on salivary alpha
amylase activity.

Course No.BT 521 Molecular Biology and Molecular Genetics Credits: 5
Lectures =
1. What is Molecular Biology? DNA as the hereditory material. RNA can also be
the hereditory material, but only in some viruses.
Determination of radioactivity. = 1
2. Size of natural DNA molecule.
Estimation of DNA
Difference between DNA and RNA. Presence
of phosphodiester linkage in RNA and DNA.
5’ to 3’ linkage.
Double strandedness of cellular DNA. =1
3. Antiparallel nature of the two strands of DNA. = 1
4. Denaturation and renaturation of DNA. Tm. GC content from Tm. Renaturation kinetics of DNA and complexity of DNA. Cot curves. =1
5. Separation of and determination of single stranded and double stranded DNA.
DNADNA hybridization relatedness of difference genes and species. = 1
6. Restriction endonuclease – an essential tool for gene cloning. DNA ligases. Plasmids. Antibiotic
resistance markers. Transformation of E. coli. =1
7. Desirable characteristics of a plasmid cloning vector. = 1
8. Centrifugation – velocity and equilibrium. Messelson & Stahl experiment. =1
9. Replication fork – John Cains experiment. Huberman
& Riggs experiment on replication of Chinese Hamster
DNA. Inman experiment on replication of lambda DNA. = 1
10. Genetic mapping – recombination frequency in bacteria
and viruses – conjugation – interrupted mating. Taylor
map. Hfr strains. =1
11. Terminal redundancy and Circular permutation in T even phages. = 1
12. DNA content in E. coli. Dichotomous replication. = 1
13. Synchronization of E. coli cells. = 1
14. Bidirectional replication in E. coli. = 1
15. Mechanism of genome transfer during conjugation Between Hfr and F strains
of E. coli. =1
16. Mechanism of Genetic recombination. = 1
17. Kornberg DNA polymerase. = 1
18. Exonuclease II and exonuclease VI as integral part of Kornberg DNA polymerase. = 1
19. Okazaki fragments. = 1
20. The Pol AI mutant. DNA pol II and pol III. Kornberg’s reappraisal of his old work. Properties of pol I, pol II and pol III. Phenotyphic defects of pol A mutant.
Ts mutants of DNA replication and genetic mapping
of the mutant loci. = 1
21. Conversion of single stranded circular DNA viruses into double stranded RF form. Synthesis of viral plus strand from RF DNA. = 1
22. OX gene A protein and its cleavage site. Rolling circle mode of synthesis. Involvement of SSB protein. =1
23. Overlapping genes. = 1
24. Insertion sequences. Transposons. =1
25. Genome organization of prokaryotes Viral genomes : General information about
different types of viral genomes. Structural organization of Retroviral genomes. =1
26. Transcription :
i. Flow of information from DNA to protein. Organization of genes in bacteria. Colinearity of genes and proteins. Operon concept. = 1
ii. Process of transcription :
RNA polymerase subunit structure and function role
of sigma factor in differential expression of genes in
bacteria. = 2
Transcription units and Cis elements. Promoter:

Consensus sequences affecting the promoter function. Constitutive and inducible promoters. Operator sequences as regulatory cis sequences. = 2

Initiation : Interaction of polymerase with the promoter and control at initiation. Attenuation. Elongation. Termination : Rho dependent and Rho independent termination. Control at termination : Attnuation. Antitermination. = 3
Processing of primary transcripts in prokarytoes
Processing of tRNA and rRNA. Cleavage of T7 early
mRNAs by RNase III. Control at the processing level. = 1
iii. Regulation of transcription in bacteria : Introduction and repression. Repressor as a regulatory molecule. Coordinated control of gene clusters. Positive and
negative regulation : Regulation of transcription of lac, trp, ara, his, and gal operons. Regulation through catabolite repression. CAP protein as a positive control factor. = 4
iv. Transcriptional regulation in bacteriopohage Lambda.
Lytic and Lysogenic switch. Role of various regulatory
proteins. =2
v. Sequential expression of genes in Bacteriophage T4, T7, Mu, x 174 : Genome organization and infection. =2

27. Translation : = 6
Genetic code and codon bias. Essential components of translation. Ribosome : the site for translation, subunit composition and assembly. Role of ribosomal RNA in translation. tRNA : Salient features of tRNA. Aminoacyl Trna synthetases. Difference between
initiator fmett RNA and mettRNA, Suppressor tRNAs, frameshift suppression.

CodonAnticodon recognition : Wobble hypothesis.Process of translation : Activation,
Initiagtion, elongation translocation and termination. Factors involved in various steps.Peptidyltransferases. Transport of bacterial proteins : Cotranslational
and Post translational mechanisms. Control of gene expression at translational level.
TOTAL LECTURES = 48

Course No.BT 522 Bioprocess Technology Credits: 3
Lectures =
Growth Rate Analysis = 2
Growth rate parameters : Specific growth rate, doubling
time, validity of exponential growth law, growth yield,
metabolic quotient, Effect of substrate concentration, Monod
Kinetics, Determination of Ks, Definition of lag period.
B. Estimation of Biomass =1
Factors influencing choice of method; Dry and wet mass,
volume, yields, metabolic rates light scattering cell count.
C. Stoichiometry = 2
Balance equation, carbon, Nigrogen balance, oxidation
– reduction principles, product formation.
D. Batch & Plug Flow Culture = 2
Open and closed systems, growth phases, Mathematical
model of simple batch culture, variations in actual practice
plug flow culture with and without feedback.
E. Chemostat Culture = 3
General principle, Balance equations critical dilution rate,
Biomass productivity, comparison with batch cultures,
residence time distribution, Test of validity, imperfect mixing,
wall growth Transient state analysis.
F. Elaboration of Chemostal = 3
Turbidostat, pH stat, D.O. stat cultures control mechanisms,
Biomass feedback Internal and External, Chemostat in
series Applications.
G. Computer Simulation = 3
Programming with ISIM, writing model equations, Material
balance concepts, Kinetic expressions.
H. Energy Requirements = 2
Electron transfer concept; maintenance energy, magnitude
and control of maintenance energy, Effect of maintenance.
I. Product Formation in Microbial Cultures = 2
Growth associated and nongrowth
associated Kinetics, Product decomposition, Balance equations for batch and
continuous systems, Effect of environmental conditions.
J. Effect of Inhibition and Activation of Growth = 2
Competitive and noncompetitive inhibition, Product and
substrate inhibition, activators, Effect on batch and
continuous systems.
K. FedBatch Culture = 2
Analysis, repeated fedbatch
culture applications, dialysis
culture.
L. Mixed Cultures = 2
Different models and their analysis.
M. Oxygen Demand and Supply = 2
Oxygen demand, solubility, measurement of D.O.T. Redox
potential oxygen transfer, measurement of KLa.
N. Aeration and Agitation = 3
Agitation and mixing, Baffled, vortex and airlift systems,
Impeller design, Effect of stirring, sparging and other
parameters.
O. Scale up Principles = 2
Methods of scale up and their analysis.
P. Process Control = 3
Measurement and control of bioprocess parameters like
temp., D.O., speed, pH, antifoam etc., Basic principles of
feedback control, Proportional, Integral and derivative
control.

Course No.BT 523 Engineering Principles Credits: 2
Basic Chemical Engineering calculations. Material balance. Material balance with reactions.
Material balance with recycle and purge. Energy balance. Enthalpy, specific heat, mean specific
heat .Heat Balance. Heat of reaction and heat of solution. Material and Energy balance together.
Fluid statics.
Fluid mechanics. Potential flow. Newtonian and non Newtonian fluid.
Bingham plastic, pseudo plastic, dilatant.
Time dependent flow
Continuity equation.
Derivation of Bernoulli Equation .Correction for friction losses.
Pump work
Skin friction and fanning friction factor. Laminar flow in pipes.
Hagen Poiseuille Equation . Hydraulic diameter
Flow of incompressible fluid in conduits and thin layers.
Friction loss due to expansion, contraction and fittings.
Flow past immersed bodies. Drag coefficient, terminal velocity. Free and hindered settling.
Metering of fluid flow.
Transportion of fluid. Pumps and valves.
Elementary idea of heat and mass transfer.

Course No.BT 524 Laboratory TechniquesII Credits: 4
Molecular Biology
Insertion mutation of a cloned gene
Large/Medium scale isolation of an E. coli plasmid (pUC19 and pUC7 KAPA).
Estimation of amount of plasmid isolated.
Restriction mapping of the plasmid pBR322.
Isolation of a gene (neomycin phosphotransferase) from the plasmid pUC7 KAPA.
Cloning of the BamHI fragment containing the neomycin phosphotransferase gene into
the BamHI site of pUC19 B/W screening.
Transformation of E. coli DH5 ( ) w ith pUC19 and also with pUC19 containing a
mutated tetracycline resistance gene.
Isolation of plasmid from the selected transformants by the “miniprep” method.
Restriction analysis of the plasmid to locate position of the insert.
Expression of Bgal
under different promoters T7 system and pUC19 (lac promoter),
with wild type E. coli as control.
Immunology
Purification of Immunoglobulin from serum
Generation of antibody in mouse
Double diffusion
Conjugation of antibodies with Enzyme
ELISA : i) Capture ELISA
ii) Direct ELISA
Western blot
Affinity column and purification of antigen
Cell fusion for generation of Hybridoma

Course No.BT 531 Computational BiologyII Credits: 2
Introduction to Molecular Structures:
Concept of external and internal coordinates and algorithms for their interconversion.
Different representations of molecular structures and their relative merits and demerits.
Experimental Methods for Molecular Structure Determination:
Brief account of structure determination by Xray
crystallography and NMR spectroscopy. Validation of experimentally obtained NMR structures. The Protein Data Bank
(PDB) and the Nucleic Acid Data Bank (NDB). The PDB and the mmCIF file formats for the
storage and dissemination of molecular structures.
Conformational Analysis:
Concept of free energy of molecules. Introduction to various force fields and their
relative merits and demerits. Techniques for Molecular energy minimization, Monte Carlo and
Molecular Dynamics simulation.
Molecular Modelling:
Methods of molecular modeling including homology modeling, threading and ab initio
protein structure prediction together with their relative merits and demerits. Methods for
structurestructure
comparison of macromolecules with special reference to proteins.
Drug Design:
General ideas of drug designing, 2D and 3D QASR, concept of a pharmacophore and
pharmacophore based searches of ligand databases. Concepts of COMFA. Methods for
simulated docking.

Course No.BT 532 Molecular Biology of Eukaryotic Systems Credits: 2
1. The Cell and the Eukaryotic Genome
2. The chromosomal DNA and proteins, Repetitive and nonrepetitive
sequence, Exons, Introns.
3. Chromatin Structure :The decondensed and active chromatin. The nucleosome
4. The Nuclear Matrix
5. Eukaryotic promoters and enhancers.
6. Eukaryotic RNA Polymerases I, II and III, The CTD domain
7. Transcription complexes, general Transcription Factors minimum Basal Unit.
Fractionation and assembly of Basal Factors.
8. TBP’s (TATAbinding
Proteins) structure/function.
9. TAF’s (TBPAssociated
Proteins) structure and function.
10. Elongation and Termination.
11. Transcriptional Activators and repressors
12. Transcriptioanl activation and transcriptional repression
13. Genome wide location analysis: serial regulation of transcriptional regulators
14. Structure and function of activators and repressors.
Symmetry in Ciselement,
Helix turn Helix.
15. Zinc fingers and Leucine Zippers.
16. Chimeric activators, Squelching.
17. Protein Protein Interaction : Role of dimerization. Heterologous gene Activation : Trans&
cis inhibition.
18. DNA Structure and Gene regulation
19. Molecular chaperones and gene Expression
20. Gene expression vs gene silencing
21. RNA Processing : Processing of Precursor RNA. RNA splicing, Splicesomes, Lariat Formation.
RNA Editing.
22. Programmed cell death (PCD) Genetic pathways for PCD Anti and proapoptotic proteins
23. Apoptotic signaling in response to DNA damage
24. Oncogenes and tumor suppressor genes
Tumor suppressor gene and signal transduction
TOTAL LECTURES = 24

Course No.BT 533 Genetic Engineering& Applications Credits: 3
1. DNA: The Structure and Properties
2. The restriction Enzymes
3. The plasmids and Cosmids, Design of Cloning and expression vectors
4. The isolation of plasmid and genomic DNA
5. The construction of cDNA and genomic libraries
6. The labeling of DNA with radiolucleotides
7. The screening of libraries: Oligonucleotide, cDNA and antibody probes
8. The Southern, Northern, Western, South western, and Far western blotting.
9. Analysis of DNAProtein Interactions
10. Electromobility shift assay, Methyl Interference assay, DNase Footprinting
11. Proteinprotein interactive cloning: The yeast two hybrid system
12. PCR and its applications
13. Fidelity of DNA polymerases
14. The use of PCR in gene assembly: multiplex, nested, RT PCR, overlap extension
and SOEing
15.PCR in gene recombination: Deletion, recombination, addition, and Sitespecific
mutagenesis
16. PCR in molecular diagnostics
17/18. Detection of hepatitis, herpes, HIV, and EBV
19.The role of PCR in detecting minimum residual diseases (MRD)
20.Gene Disorder
21. Detection of mutation in neoplastic diseases
22. SSCP, RFLP, ASA, DGGE
23. MCC, RNAseA, OLA, PTT
24. Differential gene expression profiling by Microarray
25. Differential protein expression profiling
26. Recombinant protein technology : Design and use of expression vectors.
27.Expression of foreign gene in E. coli, Baculovirus and Pichia expression system.
28. Inclusion Bodies and regeneration of active proteins.
29.Method for cell synchronization.
30.Methods of introduction of DNA into mammalian cells.
31.Transient and stable integration of foreign DNA into mammalian cells,
Single cell cloning
32. The design of viral vectors : The replication competent and the replicationdeficient
retrovirus.
33. The decision of Adeno viral, unarmed Herpes and vaccinia viral vectors.
The packaging of retroviral vectors.
34. Gene knockouts in animals.
35.Gene therapy:Somatic and germ line gene therapy in vivo and exvivo
36. Design of SiRNA vectors and Gene silencing
TOTAL LECTURES= 36

Course No.BT 534 Immunotechnology Credits: 2
A. Immune System 3 Lectures
1. Immunodefficiency Conditions
2. Lymphocyte Traffic
3. Innate and adoptive immune response in protection
B. Autigen 2 Lectures
1. Antigen engineering for better immunogericty
2. Use for vaccine development
C. Antibody molecules 3 Lectures
1. Antibody engineering
2. Antibody for diagnosis
3. Antibody for therapy
D. MHC molecules 3 lectures
1. Structure of MHC molecules
2. Antigen presentation
3. Antigen presentation by non MHC molecules
E. T Cell activation 3 lectures
1. Understanding selfnonself
discrimination
2. TH Cell subpopulation
3. Organisation of T cell receptor
F. B Cell activation 3 lectures
1. B Cell receptor complex
2. B Cell maturation
3. Generation of antibody diversity
G. Cytokines 2 lectures
1. Cytokine structure and their receptors
2. Cytokine therapy
H. Complements 1 lecture
I. Cell mediated effector responses 2 lectures
J. Lymphocyte Migration and Inflamation 2 lectures
K. Hypersensitivity reactions 2 lectures
L. Infections diseases 2 lectures
M. Auto immunity 2 lectures
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