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    Lucknow University Main Building, University Road, Babuganj, Hasanganj, Lucknow, Uttar Pradesh 226007, India
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  • Approved By: UGC NAAC

M.Sc. (Biochemistry)


Duration:

2 Years

Eligibility:

Graduation

Course  Structure

Course Code

Course Title

Semester - I

BC-101

Biophysical Chemistry and Techniques

BC-102

Biological Macromolecules: Structure and Functions

BC-103

Enzymes and Intermediary Metabolism I

BC-104

Clinical Biochemistry and Physiology

BC-105

Practical  - I

  • Biological macromolecules
  • Biophysical Chemistry & Techniques
  • Clinical Biochemistry

Semester - II

BC-201

Molecular Cell Biology

BC-202

Protein Dynamics and Biological Energy Transduction

BC-203

Microbial and Environmental Biochemistry

BC-204

Molecular Biology

BC-205

Seminar I

BC-206

Practical II

  • Enzymes
  • Microbiology
  • Cell Biology

Semester - III

 

BC-301

Plant Biochemistry

BC-302

Regulation of Gene Expression

BC-303

Enzymes and Intermediary Metabolism II

BC-304

Biostatistics, Bioinformatics and IPR

BC-305

Seminar II

BC-306

Practical III

  • Biotechnology
  • Enzyme Kinetics
  • Plant Biochemistry

Semester - IV 

BC-401

Biotechnology

BC-402

Immunology

BC-403

Project by Review

 

Course Detail

Semester - I

BC-101: Biophysical Chemistry and Techniques

  • Electrochemistry: pH and buffers, potentiometric and conductometric titrations, polarography.
  • Centrifugation techniques and their applications: Differential, zonal density gradient and ultacentrifugation.
  • Electrophoretic techniques and their applications: Gel electrophoresis, isoelectric focusisng, isotachophoresis, two dimensional electrophoresis.
  • Chromatography: Adsorption, partition, ion-exchange, reverse phase, covalent, gel filtration, affinity, gas chromatography and high performance liquid chromatography, chromatofocussing, pulse field gel electrophoresis.
  • Photometry: Theory, instrumentation and applications of visible photometry, spectrophotometry (UV, visible IR) and fluorimetry.
  • Spectroscopy: Theory, instrumentation and applications atomic absorption and emission spectroscopy, plasma emission spectroscopy, nuclear magnetic resonance spectroscopy, electron paramagnetic resonance spectroscopy, electron spin resonance spectroscopy mass spectroscopy, x-ray diffraction and Raman spectroscopy.
  • Optical methods for determination of molecular structure: Absorption of polarized light, optical rotatory dispersion, hypochromism, circular dichroism and infra-red dichroism in relation to composition and structure of biomolecules.
  • Biosensors: Basic techniques, enzyme electrode, organic salt electrode, immunoelectrodes, microbial biosensors.
  • Microscopy: Phase contrast, polarizing, confocal, electron microscopy.
  • Tracer techniques: Detection and measurement of isotopes and application of isotopes in biochemistry.

 

BC-102: Biological Macromolecules: Structure and Function

  • Carbohydrates: Classification and properties of simple carbohydrates, monosaccharides, disaccharides and polysaccharides, Structural polysaccharides: cellulose and chitin, Storage polysaccharides: starch and glycogen, Glycosaminoglycans, Glycoconjugates: proteoglycans, glycoproteins and glycolipids
  • Fatty Acids and Lipids: Structure, classification and properties of fatty acids, Structure and functions of lipids: Triacylglycerides, phosphoglycerides, sphingolipids, cholesterol, steroids, eicosanoids. Lipoproteins.
  • Amino acids and proteins: Classification, chemical structure and general properties of amino acids. Covalent structure of proteins, Levels of structure of proteins, the peptide bond and its partial double bond character.
  • Primary structure of proteins: Identification of the N- and C-terminal residues, Determination of primary structure of proteins, assignment of the disulfide bonds, peptide mapping. The peptide group, Ramachandran plot, Flexibility of the polypeptide chain, three dimensional structure of proteins.
  • Secondary structure of proteins: Repetitive and non-repetitive secondary structures, α- helices, β-pleated sheets, β-turns, other helical structures. Supersecondary structural motifs: classification and structures of commonly occurring supersecondary structural motifs.
  • Tertiary structure of proteins: General structure of globular proteins, non-covalent interactions among the amino acid residues of polypeptide chains, Characteristics and rules of formation of the tertiary structure. Domains their and organization.
  • Quaternary structure of proteins: Symmetry observed in proteins, Cyclic, dihedral and helical symmetry, Rules of association of subunits, Monomers and Protomers, Determination of quaternary structure of proteins: EM, succinylation and crosslinking, Quaternary structure determination of aspartate transcarbamoylase (ATCase)
  • Structure and functions of RNA: Physicochemical properties of RNA, Classification, structure and functions of different types of RNAs (hnRNA, mRNA, rRNA, tRNA, snRNA, snoRNA, antisense RNA, telomerase RNA, gRNA etc.), The clover leaf and L-shaped structures of tRNA.
  • Structure and functions of DNA: Base pairing: Watson-Crick, Hoogsteen and Wobble base pairs, The salient features of the Watson-Crick model of B-DNA, The structures and helical parameters of B-DNA, A-DNA and Z-DNA. Melting temperature (Tm), Forces stabilizing the B-DNA.
  • Types of nucleic acid sequences: Direct repeats, mirror repeats, inverted repeats etc., Secondary structures: bulges, bulge loops, stem-loops, cruciform etc.
  • Tertiary strand interactions in nucleic acids: paranemic and plectonemic joints, HDNA.

 

BC-103: Enzymes and Intermediary Metabolism I

  • Classification and nomenclature of enzymes, general properties of enzymes, techniques and use of enzyme assays, purification of enzymes and tests for homogeneity. Factors (pH, temperature etc.) affecting the rate of enzyme catalysis and forces involved in enzyme-substrate complex formation. Isozymes and multiple forms of enzymes. Michaelis-Menten initial rate equation based on equilibrium assumption, Briggs-Haldane steady-state approach, methods for the determination of Km,, Vmax and Kcat calculations based on Michaelis-Menten equation. Types of enzyme inhibitors and activators, qualitative analysis of data, derivation of equations for different types of enzyme inhibitors. Glycolytic and non-glycolytic pathways, hexose-monophosphate pathway, tricarboxylic acid cycle, anaplerotic sequences in metabolism, Krebs-Kornberg pathway. Transamination, deamination, decarboxylation and oxidative degradation of amino acids, urea cycle. Degradation and biosynthesis of saturated and unsaturated fatty acids. Biosynthesis of purine and pyrimidine nucleotides.

 

BC-104: Clinical Biochemistry and Physiology

  • Gastrointestinal system: Digestion and absorption of carbohydrates, fats and protein, endocrine control of digestive and absorptive processes.
  • Nerve impulse transmission: Membrane potential, action potential, transmission of nertve impulse, synthesis, storage and release of neurotransmitters, venoms and nerve poisons .
  • Muscle contraction: Structural organization of skeletal muscle; skeletal muscle contraction; actin myosin interactions; regulation of smooth and striated muscle contraction.
  • Blood: Function and composition; hemoglobinopathies; ,blood groups and Rh factor , plasma proteins and their alteration under pathological conditions; mechanism of ,blood coagulation and clot lysis ; role of leucocytes in defence against pathogens ;humoral and cell mediated immunity; immunoglobulins .
  • Respiration: Transport of respiratory gases, role of blood buffers and respiratory and renal mechanisms in acid base balance, acidosis and alkalosis.
  • Urine composition: Alterations under pathological conditions, clinical significance of urine analysis.
  • Function tests: Liver, pancreas, kidney and gut.
  • Hormones: Mechanism of action ,metabolic and physiologic role of hormones secreted by pituitary, thyroid, parathyroid ,adrenals, pancreas and gonads ,disorders due to over and under secretion; prostaglandins and thromboxanes . Biochemical and clinical aspects of AIDS, jaundice ,atherosclerosis, cancer diabetes mellitus, Alzheimers and Parkinson’s disease, hepatitis and glomerulonephritis .
  • Energy metabolism and nutrition: Balanced diet ,nutritional aspects of fats ,proteins and carbohydrates, protein calorie malnutrition, evaluation of protein quality; starvation and obesity; macrominerals and trace minerals
  • Vitamins: biochemical and physiological roles of vitamins and their deficiency diseases.

 

Semester - II

BC-201: Molecular Cell Biology

  • Membrane lipids. Physical properties of lipids and their interaction with water to form membranes. Concept of fluidity and factors causing variations in fluidity. Appropriateness of varied lipid geometry for different membrane structures. Micelles, liposomes, planar bilayers and dark membranes. Lipid rafts. Membrane asymmetry.
  • Biological membranes. Modification of lipid fluidity by membrane proteins. Arrangement of proteins within lipid bilayers. Hydropathy plots and prediction of membrane spanning domains. Organization of chloroplast and mitochondrial membrane systems.
  • Techniques to study biomembranes. FRAP, FRET, and differential scanning calorimetry. Use of spin labeling and polarity dependent fluorescence probes to determine membrane state changes. Detergents. Solubilization, purification and reconstitution of membrane protein systems.
  • Membrane transport. Channels, transporters and pumps. Active and passive transport. Pand F- type pumps and ABC transporters. Ion channels and electrical properties of membranes. Voltage, ligand and mechanically gated channels. Use of patch clamping to study ion channel activity.
  • Cytoskeleton. Actin microfilaments, microtubules and intermediate fiber assemblies. Actin and tubulin dynamics and roles of modifying/accessory proteins. Roles of microfilaments and microtubules in cellular structure and function. Control of assembly through signaling processes.
  • Cell signaling. General principles of signaling switches. Receptor characteristics. Identification and characteristics of receptor proteins. G-proteins and receptor tyrosine kinase mediated signaling. Ca2+ flux and its interpretation in cytoplasm, role of Ca2+ binding proteins. Signaling pathways dependent on regulated proteolysis.
  • Intracellular vesicular trafficking. Import of proteins into E.R. and processing in the E.R. and Golgi. Mechanism of vesicle formation and fusion. Import of relevant nuclear coded proteins into chloroplasts and mitochondria.
  • The Cell Cycle. Overview and control. Cyclins, CDKs and Ubiquitin-proteasome dependent control of cell cycle. Checkpoints. Mitosis-meiosis transition and its control.
  • Apoptosis. The role of programmed cell death in maintaining the social order of cells and in tissue sculpting. Pathways and hallmarks of apoptosis. Role of caspases and Bcl2 family proteins.
  • Cancer. Transition from normal to cancerous cell growth. Genetic instability and mutations as causative agents. Oncogenes and retroviruses. P53 and associated proteins as tumor suppressors.

 

BC-202: Protein Dynamics and Biological Energy Transduction

Protein Dynamics:

  • General aspects: Structure and assembly of fibrous protiens: keratin, silk fibroin and collagen. Protein denaturation and denaturing agents.
  • Protein folding: Introduction, thermodynamic and kinetic considerations, Folding of RNase
    • Role of protein disulfide isomerase (PDI), Renaturation of post-synthetically modified proteins: Role of the C-chain in renaturation of insulin, Role of hydrophobic amino acid residues in the folding of globular proteins, Folding pathway, Levinthal paradox and folding funnels, the concept of local and global energy minima. The multistage process of protein folding, the molten globule state. Folding pathway of BPTI (Creighton’s and Kim’s Experiments with BPTI folding)
  • Folding Accessory Protiens: Protein disulfide isomerases (PDIs) and Dsb protein, role of propeptides. Peptidyl prolyl cis-trans isomerases (PPIs), Rotamases. Molecular chaperons: Heat shock proteins, the chaperonins and other chaperones.

Protein Evolution.

Biological Energy Transduction:

  • Free Energy: Basic concept, Relationship amongst ΔG, ΔH and ΔS; Relationship between free energy and useful work, solute concentration, Chemical potential and biochemical equilibria, Biochemical examples of free energy calculations; Entropy- and enthalpydriven/opposed processes, Thermodynamics of protein folding and DNA renaturation. High energy phosphate compounds: Action as energy shuttles, Excergonic and endergonic reactions, Coupling, Phosphate transfer potential, ATP as the biochemical energy currency.
  • Redox reaction: Redox potential and its scale, electron transfer and intermediates in the mitochondrial respiratory chain and their organization. Q cycles and the stoichiometry of proton extrusion and uptake, P/O ratio. Reversed electron transfer, respiratory controls and oxidative phosphorylation, uncouplers and inhibitors, Fractionation and reconstitution of respiratory chain complexes. Chemiosmotic theory, proton circuit and electrochemical gradient, proton transport, redox loop and proton pump mechanism, bacteriorhodopsin, rhodopsin as ion pump, ionophores. Light reception by chlorophylls and LHC, Energetics of oxygenic and anoxygenic photosynthetic light reactions and photophosphorylation in plants and bacteria, energy transfer between photosystems, cyclic and non-cyclic electron transport. Microsomal electron transport, superoxides, bioluminescence.

 

BC-203: Microbial and Environmental Biochemistry

Types of microorganisms, general characteristics of main group of microorganisms, criteria used in the classification of microorganisms . Nutrition and growth of microbial cells.

  • Gram positive and Gram negative organisms : structure and function of peptidoglycan in gram positive and gram negative organisms, functions of polymeric components in outer membrane, acidic polymers in gram negative organisms, biosynthesis of bacterial cell wall.
  • Special feature of bacterial metabolism: Entner- Doudroff (ED) Pathway, modified Ed pathway, methanogenesis, Sulphur and iron utilizing bacteria. Food spoilage, fermentation, food borne infection, antibiotics, pathogenic microorganisms. Toxins produced by bacteria pathogenicity, virulence, infection. Role of microorganisms in nitrogen, carbon ,sulfur and phosphorus cycles. Biological nitrogen fixation: overview, symbiotic nitrogen fixation, nitrogenase system, ammonia assimilation.
  • Xenobiotic biotransformation: Phase I and Phase II reactions, cytochrome p-450 system Toxicity: acute, chronic, LC50, LD50, model organisms used in environmental monitoring . Air pollution : Sources, smog, suspended particulate matter (SPM), air quality, analysis of air pollutants, permissible levels acid rain, effects of air pollution on flora , fauna and human beings, control of air pollution, odour pollution.
  • Water pollution : sources, permissible levels ground water pollution, surface water pollution, water bodies pollution, marine pollution, , waste water management, effluent treatment methods, BOD. COD, control of water pollution.
  • Soil pollution: sources, soil erosion, remedial measures for soil pollution, bioremediation. Green House Effect: green house gases, global warming, threats to environment. Chloroflourocarbons (CFC): sources, ozone layer, mechanism of ozone depletion, harmful effects of ozone depletion, CFC substitutes.

 

BC-204: Molecular Biology

  • DNA topology: DNA supercoiling, Linking number, twist and writhe.
  • Organization of DNA in chromosomes: the dynamic structure of chromatin. Structure of histone core. Histone association with DNA.
  • DNA melting and reassociation kinetics: classes of DNA sequences, Cot curves. Analysis of DNA complexity.
  • DNA replication: Modes of DNA replication, Components of cellular replisomes and their functions (helicase, ligase, primase, topoisomerase, RNase H, SSB proteins, DNA polymerase etc.). The replicon, types and activities, association with prokaryotic DNA polymerase and their functions, SOS response, subunit structure and processivity of DNA polymerases. Origin of replication in prokaryotes, Eukaryotic origin of replication, Licensing factors and control of eukaryotic replication, Replication of telomeric DNA,
  • Gene stability, DNA damage and DNA repair: DNA repair enzymes, Photoreactivation; Nucleotide excision repair; Mismatch correction; SOS repair
  • Transcription in prokaryotes: Introduction, promoter architecture, subunit structure of RNA polymerase, role of σ factor in initiation of transcription, alternative sigma factors and their physiological functions, Termination of transcription, role of the ρ factor.
  • Antitermination in bacteriophage lambda (λ): Roles of pN and pQ protiens, nut and qut sites and the products of nus genes (NusA, NusB, S-10 and NusG).
  • Transcription in eukaryotes: Introduction, Transcription factors: General, upstream and inducible transcription factors; Types of RNA polymerases and architecture of their promoters. Initiation of transcription by RNA polymerase I, II and III. Elongation and termination of transcription; Enhancers and activators.
  • Genetic code: Universal genetic code; Evidence for triplet genetic codes, features of the genetic code, Degeneracy of codons; Termination codons; Isoaccepting tRNA; Wobble hypothesis; Genetic code in mitochondria;
  • Translation and transport: Adaptor role of tRNA, amino acyl tRNA synthetase, anticodon loop, direction of protein synthesis, A and P sites, initiation codon, formation of 70 S initiation complex, role of initiation in factors, peptidyl tansferase, translocation and elongation factors, stop codon, role of termination factors. Co- and post-translational \modifications, various prost-translational processing events. Transport of proteins and molecular chaperones, Protein stability, Protein turnover and degradation.
  • Transposable elements: Transposons of bacteria-IS, composite transposons, Tn transposons.
  • Transposons of Drosophila: P and Copia, Transposons of maize: Ac, Ds, Spm (En), dSpn, Retrotransposons.
  • Introductory genomics: Structural organization of genome in Prokaryotes and Eukaryotes; Organelle DNA-mitochondrial, chloroplast; DNA sequencing principles and translation to large scale projects; interpretation of DNA and RNA sequences; Recognition of coding and non-coding sequences and gene annotation; Tools for genome analysis-RFLP, DNA fingerprinting, RAPD, PCR, Linkage and Pedigree analysis-physical and genetic mapping. Genome sequencing projects.

 

Semester - III

BC-301: Plant Biochemistry

  • Secondary plant products. Biosynthesis of chlorophyll, isoprenoids and phenylpropanoids. Details of regulation of chlorophyll biosynthesis and its role in nucleus chloroplast coupling.
  • The plant cell wall. Components, structure and integration. Biosynthesis of cell wall. Indepth study of cellulose synthase action and its role in determining cell size and shape. Cell plate formation. Cell expansion.
  • Mineral nutrient acquisition. Mineral nutrient acquisition from rhizosphere. Mechanisms and strategies. Adaptation of acquisition mechanisms to mineral nutrient stresses. Hyperaccumulation.
  • Plant defense. Mechanism of plant defense against pathogens. Genetic basis of plantpathogen interactions. R-Avr gene interactions and isolation of R genes. Hypersensitive response (HR), systemic acquired resistance (SAR) and induced systemic resistance (ISR).
  • Plant photoreceptors. Rationale of photoreception and its role in regulating plant responses. Structure, diversity and function of phytochrome, cryptochrome and phototropin.
  • Phytohormones. Mode of action of auxins, gibberellins, abscissic acid, ethylene, cytokinins, Introduction to brassinosteroids, Jasmonates, oligosachharins, salicylic acid, systemin and phytosulfokines.
  • Photosynthetic energy transduction. Electron transport, light energy conversion and its control of carbon fixation. Points of cross-talk between electron transport and carbon fixation pathways.
  • Carbon fixation. Carbon fixation/ assimilation through C3 (Calvin cycle) and control of metabolite flux through the cycle. Details of Rubisco structure, assembly, catalysis and  regulation. Other regulatory enzymes of Calvin cycle. Light regulation of Calvin cycle.
  • Photorespiration. Photorespiration and carbon concentrating mechanisms (C4 metabolism and CAM). Role of metabolite transporters in regulating inter-organellar carbon flux.

 

BC-302: Regulation of Gene Expression

Basic concept and necessity of regulation of gene expression in prokaryotes and eukaryotes. Principal levels at which regulation is exercised.

Regulation of gene expression in prokaryotes:

  • Regulation of gene expression by substitution of the σ factor: Regulation of gene expression during heat shock response, nitrogen starvation, chemotaxis and following infection of Bacillus subtilis by bacteriophage SPO1.
  • Regulation of gene expression by antitermination: Regulation of expression of the phage λ genes upon infection of the E. coli host, Factors and elements involved in antitermination.
  • The operon concept: Positive and negative control of gene expression, the operon, inducible and repressible operons. The lac operon: repressor control and catabolite repression. The trp operon: repressor control and attenuation. Regulation of transcription by small RNA molecules, Stringent response.

Regulation of gene expression in eukaryotes:

  • Maturation of 5’ and 3’ ends of mRNA: Capping, cleavage and polyadenylation, maturation of 3’ ends of histone mRNAs, Functions of the cap and the poly A tail of eukaryotic mRNAs.
  • MRNA splicing and regulation of gene expression: Exons and introns, classification and properties of introns. Autocatalytic splicing, splicing of Group II and Group I introns. Splicing of nuclear pre-mRNA introns, splicing pathway, the spliceosome, roles of snRNPs, splicing factors. Splicing enhancers and splicing repressors. Alternative splicing, mechanism of alternative splicing and its regulation, role of alternative splicing in sex determination of Drosophila melanogaster.
  • DNA-protein interactions: Physico-chemical characteristics of DNA-protein interaction, Sequence specific binding of DNA. DNA binding motifs: Zinc fingers, basic Leu zipper (b/zip), basic helix-loop-helix (b/HLH), b/HLH/zip motifs. Techniques for study of DNAprotein interaction.
  • Activation of transcription factors: Types of transcription factors; mechanisms of activation of transcription factors; Regulation of many genes by a single transcription factor; Regulation of a single gene through different circuits; Combinatorial principle of gene expression.
  • Control of gene expression by chemical modification of DNA: Types of chemical modificaitons, Determination of DNA methylation pattern, DNA methylation and gene expression, CpG islands; Maintenance methylation.
  • Control of gene expression by histone modificaiton: Histone acetylation, deacetylation and phosphorylation. Enzymes associated with these modifications (HATs, HDACs etc.). Coactivation and repression complexes; The bromodomain and chromodomain protiens; Histone code hypothesis.
  • Control of chromatin structure: Chromatin remodeling as an active process, remodeling changes in chromatin, DNase I hypersensitive sites, the chromatin remodeling complexes of yeast.
  • Genomic Regulatory domains: Regulation of expression of gene clusters; Locus control region: Structure and function, LCR of mouse β-globin gene cluster; Insulators: Structure and functions, the insulators of hsp70 genes of Drosophila melanogaster; Genomic imprinting.

 

BC-303: Enzymes and Intermediary Metabolism II

  • Two substrate systems: Kinetic mechanisms Sequential and ping-pong pathways, Cleland representation and nomenclature, Form of initial rate equations for random, ordered and pingpong pathways and their primary and secondary plots.
  • Regulation of Enzyme activity: Feedback inhibition, allosteric concept, qualitative description of concerted and sequential models, Negative cooperativity and half-site reactivity, Flip-flop mechanism, Hill and Scatchard plots, Covalent modification.
  • Mechanism of enzyme action: The concept of active site, Proximity orientation effect, strain and distortion theory, Acid-base catalysis, covalent catalysis, Chemical modification, techniques for studying the mechanism of action, general mechanistic principles.
  • Physicochemical properties and mechanism of action of enzymes: Alcohol dehydrogenase, chymotrypsin, lysozyme and hexokinase.
  • Enzyme technology: Immobilization and applications. Control of carbohydrate metabolism
  • Metabolism of neutral and polar lipids: Glyderides, phospho-, sulfo-, galactolipids and cerebrosides, Control of lipid metabolism. Physiological control of metabolic flux, evidence of multisite modulation and its implication in relation to carbohydrate and lipid metabolism. Biosynthesis of amino acids and its regulation. Biosynthesis of coenzymes.

 

BC-304: Biostatistics, Bioinformatics and IPR

Biostatistics:

  • Introduction to Biostatistics: Aims and scope of statistics in biological sciences, Basic definitions and applications, Sampling and sampling techniques.
  • Data collection and presentation: Types of data, methods of collection and graphic representation of data.
  • Measures of central tendency: Mean, Median, Mode.
  • Measures of variability: Standard deviation, standard error, mean deviation and coefficient of variation. Correlation and regression, Linear regression and regression equation.
  • Tests of significance: Chi-square test, t-test, Z-test and standard error. Introduction to probability theory and distribution.

Computer Applications and Bioinformatics:

  • Introduction to computers: basic organization of computers, CPU and input and output devices, Personal Computers, Mainframes and Supercomputers, hardware and software. Introduction to Windows as an operating system, file and folders, commonly used commands. Basics of common application software packages for Word processing (MS Word), spreadsheets (MS Excel) and presentation (MS Power point). Introduction to internet, Medline and Pubmed for accessing biological information. Introduction to Bioinformatics, Accessing and retrieving sequence information from genome sequence databases, use of genomic data. Overview of comparative and functional genomics, Introduction to protein modeling and proteomics.

Intellectual Property Rights:

  • Types of IP: Patents, Trademarks, Copyright & Related Rights, Industrial Design, Traditional Knowledge, Geographical Indications, IPs of relevance to Biotechnology. Salient features of Indian Patent Act 1970 and recent amendments. Introduction to Patents; Types of patent applications. Patent databases.

 

Semester - IV

BC-401: Biotechnology

  • Modification and restriction: DNA methylation, restriction endonucleases, Class I, II and III, nomenclature, general properties, mode of action. Formation of chimeric plasmids using restriction enzymes, homopolymer tailing, synthetic linkers and adaptors.
  • Blotting techniques: Overview, selection and screening of recombinants, genetic, nutritional, immuno0logical blotting. HART and HAT.
  • DNA libraries: Genomic and cDNA libraries, cDNA synthesis and cloning, chemical synthesis.
  • Plasmid cloning vectors: plasmid types, modular organization of plasmid, control of copy
  • number, properties of ideal plasmsid cloning vector.
  • Phage as a cloning vector: advantages in the use of phage lambda, cosmid cloning, other useful phages used as cloning vectors, e.g., M 13, cosmids and phagemids.
  • Cloning in yeast: basic principles of development of yeast vectors, YEP, YRP, YIP, selection and expression of clones.
  • Cloning in plants cells: methods for gene transfer in plants, caulimoviruses, Ti-plasmid, TDNA structure and transfer mechanism, selection marker genes and reporter genes, binary vector system.
  • Cloning in mammalian cells: viral vectors, shuttle vectors of other viruses. Examples of cloned mammals.
  • Recombinant DNA technology: applications in agriculture, medicine and industry.
  • Enzyme and protein engineering, site directed mutagenesis.
  • Industrial applications of enzymes, enzyme immobilization techniques and significance.
  • Fermentation biotechnology: bioreactors, industrial production of alcohol.

 

BC-402: Immunology

  • The Immune system: basic concepts of innate and acquired immunity types of acquired immunity; innate host defense; clonal selection hypothesis; components of the immune system ; hematopoiesis ; inflammation and phagocytosis.
  • Cells of adaptive immunity: lymphoid organs and tissues .T and B lymphocytes; APCs; lymphocyte recirculation and homing: primary and secondary lymphoid organs. MALT and other lymphoid tissues.
  • Antigens and antibodies: immunogens, antigens and haptens; epitopes; B and T cell recognition of antigen; cross-reactivity; immunoglobulin classes and sub-classes ; general structure of antibody; isotypes; idiotypes; allotypes; structure and biological properties of antibody isotype; immunoglobulin superfamily; primary and secondary humoral response, polyclonal and monoclonal antibodies; chimeric and humanized antibodies; abzymes; antigen-antibody interactions.
  • Cytokines: general properties; functional classification; cytokine receptors and signal transduction; pathophysiology; use of cytokine/cytokine receptors in therapy and diagnosis, Interferons and their applications.
  • The Complement system: biological role of the complement system; complement components; various pathways of complement activation; regulation of the complement system; complement deficiencies.
  • Antigen recognition by lymphocytes and development of the immune repertoire: BCR; TCR; maturation of B and T lymphocytes; mechanisms of diversity in antigen receptors ; MHC: class I and class II MHC molecules; antigen processing and presentation ; superantigens ; T cell responses to lipid and glycolipid antigens.
  • Cell-mediated immunity: phases of T cell responses; APCs and T cell interactions; T cell activation; decline of immune responses; TH 1 and TH 2 subsets; effector mechanisms of CMI.
  • Humoral immunity: Initiation of B cell responses by antigen ,TH and B cell interactions; B cell activation and antibody production; isotype switching; affinity maturation ; TI and T D antigens; effector mechanisms of humoral immunity; mucosal immunity .
  • Immune responses against microbes: immunity to bacteria, viruses, fungi, protozoa and helminths, passive and active immunity.
  • Vaccination; principles of vaccination, vaccines in current use; new vaccines in development; adjuvants.
  • Hypersensitivity reactions: Type Ð�, Ð�Ð�, Ð�Ð�Ð� and IV hypersensitivity.
  • Immunological tolerance and autoimmunity: central and peripheral lymphocyte tolerance; oral tolerance and its significance; categories of autoimmune disease; genetic factors, role of infections and other factors in autoimmunity; animal models of autoimmune disease; human autoimmune diseases; diagnosis and treatment.
  • Transplantation and graft rejection: types of grafts; transplantation antigens; immune mechanisms in graft rejection; prevention and treatment of rejection reactions; bone marrow and HSC transplantation.
  • Tumor immunology: tumor antigens; mechanisms of tumor rejection; evasion of immune responses by tumors; tumor immunotherapy.
  • Immunodeficiency diseases; congenital and acquired; HIV infection and AIDS
  • Immunological methods and applications: immunization procedures; preparation of polyclonal antiserum; antibody purification; hybridoma technology for monoclonal antibody production; surface plasmon resonance; biosensor assays for assessing ligand-receptor interactions, agglutination; precipitation reactions in gels; immunoelectrophoresis; immunoprecipitation; RIA; ELISA; biotin-avidin based immunoassays; immunofluorescence microscopy immunoelectron microscopy; immunohistochemistry; immunoblotting; complement fixation, isolation of lymphocyte populations and subpopulations; FACS; evaluation of functional activity of the defense system; lymphocyte effector function assays.