Suresh Gyan Vihar University Courses

M.Sc. (Biochemistry)

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Duration: 2 Years

Eligibility: Graduation

Course structure

Semester	Subject Code/ question paper code	Title of the subject	Marks			Duration of Exam. (Hrs)
			IA	Sem. End Exam	Total
I	I Bio BC 101	Cell Biology	30	70	100	3
	I Bio BC 102	Immunology	30	70	100	3
	I Bio BC 103	Biochemical Techniques	30	70	100	3
	I Bio BC 104	Molecular Biology and Genetics	30	70	100	3
		Practical I – Cell Biology & Immunology Practical II –Biochemical Techniques & Molecular Biology and Genetics	30 30	20 20	50 50	4 4
II	II Bio BC 105	Chemistry of Biomolecules	30	70	100	3
	II Bio BC 106	Enzyme Technology and Bioenergetics	30	70	100	3
	II Bio BC 107	Metabolism and Metabolic Regulation	30	70	100	3
	II Bio BC 108	Biochemistry of  Hormones	30	70	100	3
		Biochemistry Practical I Biochemistry Practical II	30 30	20 20	50 50	4 4
III	III Bio BC 109	Plant Biochemistry and Biotechnology	30	70	100	3
	III Bio BC 110	Microbial Biochemistry	30	70	100	3
	III Bio BC 111	Advanced Clinical Biochemistry	30	70	100	3
	III Bio BC 112	Genetic Engineering	30	70	100	3
		Biochemistry Practical I Biochemistry Practical II	30 30	20 20	50 50	4 4
IV	IV Bio BC 113	Elective paper (Independent Study )			100
	IV Bio BC 114	Dissertation/Project work	120	80	200

 

Course Detail

Semester  - I

I Bio BC: 101- Cell Biology

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours    

Total Lecture/ Paper: 60 hrs

Unit - I

Plasma membrane  

Ultrastructure of cell,cell theory,exceptions of cell theory. Membrane bilayer - Composition and structure: Models, fluidity, Liposomes. Membrane associated receptors.

Membrane proteins – types ,Flippases, protein of RBC membrane ,RBC ghost,  porins  and  aquaporin. and membrane transport system.

Unit – II

Cell organelles and secretion

Golgi, endoplasmic reticulum, lysosomes, peroxisomes. Internalization of macromolecules and particles : endo and exocytosis.

Mittochondrial structure and oxidative phosphorylation. Chloloplast and Photo phosphorylation.

Nucleus : Nuclear envelope, nucleolus, chromosomes and their structural organization, ribosomes

Unit - III

Cell division and cell cycle  

Cell cycle and its regulation, regulation of cell division Go-G1 transition check points in cell cycle,chromosome movements.

Mutation and its types ,molecular basis of mutation.

Cytoskeleton . topography,microtubules,microfilaments

Unit - IV

Signal transduction

Cell cell signaling, Signal Transduction cascades. Receptor triggerd phosphorylation cascade, G protein,G protein coupled receptor, functions of cell surface receptor, pathways of intracellular signal transduction.

Cascade, cyclic CAMP as a second messenger, protein kinases, receptor mediated hydrolysis of phosphotidyl inositol, IP3, Diacyl glycerol, calcium ion as a cytosolic messenger.

Unit - V

Cancer

Properties of tumor cells,tumor suppressor genes and carcinogenic effects of chemical and radiations

Apoptosis, difference between nacrosis and apoptosis ,pathways, regulation and effectors in apoptosis

Cell cell interaction, cell –cell adhesion ,specialized junction, desmosomes,gap junction ,adhesion molecules,cadherins and connexins

 

I Bio BC: 102 Immunology

Max. Marks: 70

Time: 3 Hours

Total Lecture/ Unit: 12 Hours    

Total Lecture/ Paper: 60 hrs

Unit - I

History of Immunology

Types of immunity – Innate and acquired - Passive and Active. Cells and Organs of Immune System:-Lymphoid cells; Stem cells, B and T Lymphocytes, Natural killer cells, Mononuclear phagocytes, Granulocytic cells. Organs: Thymus, Bone Marrow, Lymphatic system, Lymph nodes, Spleen.

Unit - II

Antigens and Antibodies

Antigenicity, immunogeuecity and Antigens :, Structure, properites, types, – iso and allo – haptens; adjuvants, Epitopes, superantigens, Immunoglobulins – structure –properties (physico chemical and biological); Monoclonal Antibodies, and Hybridoma technology

Unit - III

Antigen-Antibody Interaction

Generation of humoral and cell mediated immune response, Major Histocompatibility Complex,General structure and function of MHC,MHC Molecules and Genes ,Antigen Processing and presentation T-Cell Receptors,T-Cell Maturation and Differentiation. B-Cell Generation, Activation & Differentiation.Antibody mediated effector functions, Antibody dependent cell mediated cytotoxicity.

Unit - IV

Regulation of immune response

Cytokines and their role in immune regulation. Immune Effecter Mechanism-Cytokinesis structure ,receptor ,and function. (Properties, receptors, antagonisis & secretion) Hypersensitive reactions (Type I,II,III and delayed type (DTH) Tumor immunology, Transplantation Technology and Autoimmunity ,AIDS and other Immuno deficiencies, Vaccines -Types of vaccines-Genetically designed vaccines. BCG, TB & Leprosy, DNA vaccines, Complement system.

Unit - V

Immunological techniques and their principles

Invitro of immunological methods – agglutination, precipitation, complement fixation, immunofluorescence, ELISA,       RadioImmunoassays – Immunodiffusion, Immunoelectrophoresis  –  Isoelectric  focusing  –  cytotoxicity  assay  , Immunohistochemistry.  

 

I Bio BC 103:  Biochemical  Techniques

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit - I

Electrophoretic techniques

Principle, types and affecting factors. Instrumentation and application of paper, gel, SDS- PAGE , Isoelectric focusing, 2-DGel electrophoresis , Pulsed field gel electrophoresis and capillary electrophoresis. Membrane filtration and dialysis

Unit - II

Centrifugation techniques

Principle and technique of preparative and analytical centrifugation, differential centrifugation, density gradient centrifugation, ultracentrifuge and its application

Unit - III

Chromatographic Techniques

Principle, technique and applications of Paper, TLC, Ion-Exchange, molecular sieve, affinity chromatography and adsorption chromatography,. Gas chromatography, HPLC

Unit - IV

Spectroscopic technique

Basic principles, instrumentation and applications of UV, Visible and IR spectrophotometers. Optical Rotatory Dichroism and Circular Dichroism . Nuclear Magnetic Resonance ESR , X-Ray Crystallography and Mass Spectrometry. Flame Photometry.

Unit - V

Radio chemical methods -   Nature of radioactivity, types of radioactivity, radioactive decay, units of radioactivity. Radioisotopes: Detection and measurement of radioactivity. Geiger counters, scintillation counters, autoradiography.   Microscopy: light, phase-contrast, fluorescence and electron microscopy

 

I Bio BC 104 : Molecular Biology and Genetics 

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit - I

Introduction  to Molecular Biology and Genetics

DNA Replication. Prokaryotic and eukaryotic DNA replication, Enzymes ( Like DNA  Polymerases,Topoisomerases etc)  and accessory proteins involved in DNA replication. Inhibitors or DNA replication ( blocking precursor synthesis, nucleotide polymerziation, altering DNA structure)

DNA damage and repair: types of DNA damage (deamination) oxidative damage, alkylatoin, pyrimidine dimers). repair pathways-methyl-directed mismatch repair, very short patch repair, nucleotide excision repair, base excision repair, SOS system. Mutations: nature of mutations; mutagens

Unit – II

Transcription

Structural features of RNA (rRNA, tRNA and mRNA) and relation to function Polycistronic and monocistronic RNAs, Prokaryotic transcription, Comparison  with Eukaryotic transcription, Maturation and processing of RNA : methylation, cutting and trimming of rRNA; capping, polyadenylation and splicing of mRNA; cutting and modification of tRNA degradation system. Catalytic RNA group I and group II intron splicing RNase P.

Unit - III

Translation

Prokaryotic and eukaryotic translation, Mechanisms of initation, elongation and termination, post-translational modifications of proteins. Synthesis of Secretory and membrane proteins. Helix turn Helix. Zinc fingers and Leucine Zippers,Chimeric activators, squelching

Unit - IV

Antisense and Ribozyme

Technology,Applications of antisense and ribozyme technology.

Gene transfer mechanisms- transformation, transduction, conjugation and transfection. Plasmids, F-Factors, Colicins and col factors. Plasmids as vectors for gene cloning. Replication of  plasmids and compatibility.

Unit - V

Regulation  of  Bacterial  Gene  Expression  

Operon  model  –  lac,  ara ,and trp   operon concept, catabolite repression, positive and negative regulation, inducers and corepressors.  Negative regulation –  regulation by attenuation –  his and  trp operons;  antitermination  –  N  protein  and  nut  sites  .    Induction   and  repression  mechanism  in operons. Global regulatory responses : heat shock response, stringent response and regulation by small molecules such as ppGpp and cAMP.

 

Semester – II

II Bio BC: 105 Chemistry Of Biomolecules

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit - I

Carbohydrates

Chemistry and classification of carbohydrates. Structure and physiochemical Properties of Monosaccharides, disaccharides. Stability and formation of glycosidic bond. Configuration and conformation. Polysaccharides; Occurrence, structure and biological function of Homoglycans, Heteroglycans, Mucopolysaccharides,  proteoglycans, and glycoproteins.

Unit - II

Lipids

Chemistry and Classification of lipids. Fatty acids-structure, types and their physiochemical propertie. Structure and biological role of TAG, phospholipids, sphingolipids, gangliolipids cholesterol. Bile acids and bile salts. Structure and biological role of lipoproteins, prostaglandins, prostancilins and leukotrienes.

Unit - III

Protein I

Chemistry and Physiochemical properties of the amino acids, Peptides and the peptide bond, stability and formation of the peptide bond. Proteins structure- primary, Secondary structure – Alpha Helix, Beeta Sheet, 310, Pie helix, Super secondary structure. Ramchandran plot . Tertiary structure and quaternary

structure – Silk Fibrion , collegen, Haemoglobin , Lysozyme , Rnase and Myoglobin

Unit - IV

Protein II

Amino acid analysis of proteins. Primary structure, determination of the N and C terminal residues of a protein, sequence determination of a protein. Force stabilizing protein structure. Effect of temperature, salts, acids and alkali solution on protein structure. Protein structure analysist by ORD, CD, NMR, and X Ray Crystallography. Peptide Synthesis – Solution and solid phase methods. Introduction to DNA- proteomics.

Unit - V

Nucleic Acids

Chemistry of Nucleic acids. Structure and composition of nucleic acids. Types of  DNA (B, A, C and Z forms). Forces stabilizing nucleic acid structure. DNA bending –wedge and junction model , super coiled forms of DNA. Effect of temperature, salts , acid, alkali and enzymes on nucleic acid structure. Cruciform structure and its stability. Types of RNA- Secondary and tertiary structure. Nucleoproteins. DNA – Protein interaction.   Fractionation and analysis of nucleic acids. Solution methods, chromatography, electrophoresis, centrifugation, blotting techniques and auto radiographic methods. 

 

II Bio BC: 106- Enzyme Technology and Bioener-getics

Max. Marks: 70 

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit – I

Enzyme: Historical aspects, classification and nomenclature, EC number.  Mechanism of enzyme catalysis and action. Sub cellular localization and organization of enzymes.  Methods of enzyme assay: continuous and sampling techniques, coupled enzyme assay and methods and significance of enzyme turnover number; specific activity

Unit - II

Enzyme purification techniques : objectives and strategy; methods of homogenization; method of isolation; purification and crystallization  Criteria of purity and tabulation of purification data; stable storage of enzymes  Characterization of purified enzyme. Coenzymes, Cofactors and Isoenzymes

Unit - III

Enzyme Kinetics: Equilibrium and steady state theory, rate equation and determination of Km and Vmax. Factors affecting rate of enzyme reaction: pH, temperature and pressure. Enzyme inhibition: reversible and irreversible inhibition, their type, inhibitor constant and its significance. Rapid reaction techniques  

Unit - IV

Protein- ligand binding: types, cooperativity, Hill and Scatchard plot, Allosteric enzymes: Models of allostery, types and kinetics. Regulation of enzymes Mechanism of action of Chymotrypsin; Ribonucleases; Lysozyme; Metallo-enzymes. Degradation of enzymes

Unit - V

Enzyme immobilization; techniques; experimental procedures and effect of immobilization on kinetic parameters. Principle and Industrial application of immobilized systems. Enzymes in Medical diagnosis and enzyme therapy. 4. Enzymes during aging

 

II Bio BC: 107-Metabolism and Metabolic Regulation

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit - I

Metabolism of carbohydrates- glycolysis, citric acid cycle and its regulation high lighting the following key enzymes- hexokinase, phosphofructokinase and pyruvate dehydrogenase complex. Pentose phosphate pathway, glucoronic acid pathway, gluconeogenesis, glyoxylate cycle, glycogenesis and glycogenolysis. Regulation of glycolysis and gluconeogenesis. Metabolism of amino sugars, sialic acids, mucopolysaccharides and glycoproteins.

Unit - II

Chemical nature of fatty acids and acylglycerols- sources and biological functions. Biosynthesis of fatty acids, hydroxy fatty acids and acylglycerols. Methods of inter-organ transport of fattyacids and their primary products. Biosynthesis of phospholipids and their biological functions. Utilization of fatty acids for energy production, alpha, beta and gamma oxidation of fatty acids. Formation of ketone bodies. Peroxisomal oxidation of fatty acids.

Unit - III

Derived lipids: Biosynthesis of cholesterol, its regulation and excretion. Biosynthesis of sphingosine, ceramides, sphingomyelin, cerebrosides, gangliosides, prostaglandins, thromboxane, eicostatetraenoic acid and leucotrienes. Lipoproteins- Types and biological functions.

Unit - IV

Oxidative degradation of amino acids : Proteolysis, Transanimation, oxidative deamination, acetyl CoA, Alpha ketogutarate, acetoacetyl CoA, succinate, fumarate and oxaloaccetate pathway, decarboxylation, urea cycle, Ammonia excretion. Biosynthesis of amino acids: Amino acid biosynthesis, Precursor functions of amino acids, Biosynthesis of aromatic amino acids, Histidine, One carbon atom transfer by folic acid (Biosynthesis of glycine, serine, cysteine, methionine, threonine).  Peptides, polyamines, Porphyrins, gamma glutamyl cycle, glutathione biosynthesis, Nonribosomal Protein Biosynthesis.

Unit - V

Synthesis of purine and pyrimidine – de novo and salvage pathways. Synthesis of deoxy and oxy-ribonucleotides,. Inhibitors of nucleotide synthesis and their role in chemotherapy.

Biosynthesis of nucleotide coenzymes. Nucleotide degradation- catabolism of purines and pyrimidines. Disorders in purine and pyrimidine metabolism.

 

II Bio BC: 108 - Biochemistry of hormones

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit - I

Introduction to endocrine gland. Hormone classification on the basis of chemical nature and mechanism. Mechanism of hormone action, hormone receptors, role of second messengers, hormone and homeostasis, local hormones and feedback regulation of hormone.

Unit - II

Pituitary gland –Endocrine hypothalamus- secretion and physiological roles of hypothalamic releasing and inhibitory factors. Biosynthesis, mechanism of action, physiological roles and regulation of anterior and posterior pituitary hormones. Pituitary endocrinal disorders. Pineal gland –synthesis, mechanism of action and functions of melatonin.

Unit - III

Thyroid gland – Biosynthesis, mechanism of action, regulation and physiological role of thyroid hormones. Hypothyroidism and hyper thyroidism. Parathyroid gland –biosynthesis, regulation and physiological role of parathyroid hormones. Hormonal regulation of calcium metabolism.

Unit - IV

Endocrine pancreas –Chemistry, mechanism of action and physiological roles of insulin, glucagon, somatostatin and pancreatic peptide. Hormones of Gastrointestinal tract.

Adrenal gland- Biosynthesis, mechanism of action, regulation and physiological roles of adrenal hormones. Adrenal hormones disorders.

Unit - V

Reproductive Endocrinology – Male sex hormones –synthesis, mechanism of action, regulation and physiological roles of androgens.

Female sex hormones –Biosynthesis, mechanism of action, physiological roles and regulation of ovarian hormones. Placental hormones, hormonal regulation of pregnancy, menstrual cycle and lactation.

 

Semester – III

III Bio BC 109-Plant Biochemistry and Biotechnology

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours    

Total Lecture/ Paper: 60 hrs

Unit - I

Overview of photosynthesis: Light absorption and energy conservation, Light properties of both particles and waves. Light absorbed by pigment molecules. Light reaction center complex. The photo system, organization of thyllakoid. Electron transport pathways in chloroplast membranes. ATP synthesis in chloroplasts. Carbon reactions C3, C4 and CAM plants. and  Photorespiration

Unit - II

N2 fixation - Enzymology of N2 fixation. Symbiotic N2 fixation, Non- symbiotic fixation. Interaction between nitrate assimilation of carbon metabolism. Reductive sulfate assimilation pathway. Biochemistry of photoperiodism and seed dormancy.

Plant hormone; biochemistry and physiological role.

Unit - III

Introduction to plant tissue culture,. Tissue culture media (composition and preparation). Initiation and maintenance of callus and suspension culture; single cell clones. Organogenesis; somatic embryogenesis; transfer and establishment of whole plants in soil. Shoot-tip culture: rapid clonal propagation and production of virus-free plants. Embryo culture and embryo rescue. Protoplast isolation, culture and fusion; selection of hybrid cells and regeneration of hybrid plants; symmetric and asymmetric hybrids, cybrids .Production of haploid plants through tissue culture technique.

Unit - IV

Introduction to animal biotechnology. Cells and cell lines, media for cell structure and equipment.  Equipments and materials for animal cell culture technology. Primary and established cell line cultures. Monoclonal antibodies. Immunotoxins as therapeutic agents Stem cell culture, embryonic stem cells and their applications.  

Unit - V

Gene transfer in plant; Physical and chemical methods.   Agrobacterium and Ti plasmids, Ti- Binary vectors. Plant viruses as vectors. Transgenic plants - application, methods of engineering insecticide and herbicide resistant plants. Anti-sense RNA technology - altering nutritional contents of plant foods.

 

III Bio BC 110-Microbial Biochemistry

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours    

Total Lecture/ Paper: 60 hrs

Unit - I

Isolation, cultivation and identification of bacteria. The bacteria cell wall structure. Gram positive and gram negative bacteria Microbial nutrition and growth. Bacterial growth and kinetics. Chemostatic culture Continuous cultivation of microbes,

Unit - II

Fermentation – Types of fermentation processes- Batch,continous and fedbatch  culture.Alcoholic fermentation, lactic acid fermentation. penicillin, riboflavin, glutamic  acid,lysine, amylases and proteases Solid state fermentation. Sterilization and scale- up process

Unit - III

Basic design of fermentors. current design of stirred tank reactor, aspetic operation, control systems, batch versus continuous operation,  Tower fermenter, Air lift fermenter. .  Aeration and Agitation. Agitation and mixing, Baffled, vortex and airlift systems, Impeller design, Effect of stirring, sparging and other parameters. Down-stream processing.

Unit - IV

Production of biomass (microbial insecticides,starter cultures, single cell proteins production). Production of low molecular weight compounds-primary and secondary metabolites. Metabolic end products. Bioconversions. Microbial polysaccharides. Production of enzymes (amylases proteases, lipases and cellulases) and high fructose syrup Microbiological mining Introduction to drug design.

Unit - V

Antibiotics: Chemistry and biosynthesis of important antibiotic compounds. First, second, third and fourth generation antibiotics with reference to modified penicillins.Antibiotic resistence. Biochemical modes of action of antibiotics acting as inhibitors of ribosomal function (e.g., aminoglycosides, tetracyclines, puromycin, chloramphenicol etc.) inhibitors of nucleic acid metabolism, actinomycin D, mitomycin C etc. inhibitors of cell wall biosynthesis (penicillins, bacitracins etc.) and inhibitory of membrane function (polyenes, peptide antibiotics etc.)

 

III Bio BC 111- Advanced Clinical Biochemistry

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours

Total Lecture/ Paper: 60 hrs

Unit – I

Blood coagulation – its mechanisms, clotting factors and disturbances in blood clotting - Haemophilia A and Haemophilia B. Anticoagulants. Blood groups, Haemoglobin in anaemias, Sickle cell anemia, Thallasemia, abnormal haemoglobins identifications, Systematic analysis of haemorrhage disorders. Porphyrias and porphyrinurias. Blood banking. Hemolytic diseases of the new born. Adverse reactions of blood transfusions.

Unit - II

Blood sugars – Its maintenance, hyper and hypoglycemia. Regulation of blood glucose concentration – Diabetes mellitus – Complications, secondary degenerative diseases. Laboratory diagnosis of early and latent diabetes. Glucose tolerance test. Dietary regimes in diabetes mellitus. Hypoglycemic agents. Galactosemia, Fructosuria and lactose intolerance. Hypo and hyper cholesteremia, Hypo and hyper lipoprotenemia, Hypocholestremic agents, Hypertension. Lipid storage diseases, fatty liver, obesity.

Unit - III

Protein deficiency diseases, plasma proteins, their significance and variation in health and diseases. Agammaglobulinemia, Multiple myeloma, Proteinuria, Wilson’s disease – Gout leshnyan syndrome. oratic aciduria, and xanthinuria, cystinuria, Hartnup disease, Mapple syrup disease, alkaptonuria, albinism, Tyrosinosis, Phenylketonuria. Disorders of sulphur containing amino acid and urea cycle.

Unit  - IV

Normal structure and functions of Liver - Diseases of the Liver - Hepatitis - types, Jaundice and varieties. Cirrhosis, Alcoholic liver diseases. Cholestatic liver diseases. Hepatic Tumors and Biliary tract diseases - Clinical manifestation of liver diseases. Liver functions Tests. Disorders of Bilirubin metabolism. Enzyme released from diseased liver tissue. Hepatoprotective role medicinal plants. Pancreatic function Test; Gastric function Test. Biochemical parameters of CSF in health and disease.

Unit - V

Renal function tests - biochemical changes in acute and chronic renal failure. Normal and abnormal urinary constituents. Renal stress and its analysis. Enzyme parameters in pathological conditions. Cardiac pathology - Major manifestations of heart disease - Ischaemic heart diseases, Angina pectoris, myocardial infections. Cardiac markers in infection - LDH, Creatine kinase. Serological tests in infectious diseases . Serological diagnosis of viral infections. Amniotic fluid and maternal serum, ailment in pregnancy.

 

III Bio BC 112-Genetic Engineering

Max. Marks: 70

Time: 3Hours

Total Lecture/ Unit: 12 Hours    

Total Lecture/ Paper: 60 hrs

Unit - I

Scope of Genetic Engineering ,Milestones in Genetic Engineering - Core techniques (Blotting techniques, electrophoresis and  Autoradiography) and essential enzymes used in rDNA technology-- Restriction enzymes,modifing enzymes - Ligases ,DNA and RNA polymerases Terminal transferase ,Molecular Markers ,Nucleic Acid  isolation ,separation , Purification, Yield Analysis.

Unit - II

Cloning -Principles of gene cloning, Types of cloning,. Gene Cloning Vectors- Plasmids, bacteriophages, phagemids, cosmids. Artificial chromosomes, Shuttle vectors. cDNA Synthesis and Cloning -- mRNA enrichment, reverse transcription, Linkers and adaptors.

Unit – III

Library construction and screening -Genomic, Chromosomal, cDNA Library. Restriction Mapping of DNA fragments. The labeling of DNA with radiolucleotides Screening of libraries: Oligonucleotide, cDNA and antibody probes, Analysis of DNA-Protein Interactions. Electro mobility shift assay, DNA Foot printing. Methods of DNA and genome Sequencing DNA transfection methods, Primer extension method, SI mapping, RNase protection assays, Reporter genes and their assays. Cloning    interacting genes. Two and three hybrid systems, cloning differentially expressed genes. Nucleic   acid   microarray arrays. Chromosome walking.

Unit - IV

PCR, types and its applications .Multiplex, Nested, RT- PCR. Site-directed Mutagenesis and Protein Engineering.

Unit - V

Recombinant protein technology : Design and use of expression vectors, selection of suitable promoter sequences, ribosome binding sites, transcription terminator, fusion protein tags, purification tags, purification tags, protease cleavage sites and enzymes, plasmid copy number.  Processing   of Recombinant proteins- Stabilization of proteins. Phage Display, Inclusion Bodies, solubilization of insoluble proteins. Expression Strategies for Heterologous Genes- Codon optimization, expression in bacteria, expression in yeast, expression in insects and expression in mammalian cells. Gene therapy: Somatic and germ line gene therapy in vivo and  ex-vivo. Gene silencing.

Semester – IV

IV Bio BC 113- Elective Paper

The Elective paper in the M.Sc. IV Semester will be based on detailed review report on one of the courses listed in the syllabus. The student will make a complete report in about 100 pages that shall be evaluated by the course coordinator and one internal teacher. The marks will be awarded internally. It is proposed to include the following areas as part of elective papers.

1. Proteomics, functions genomics and therapeutic genomics.
2. Topics on human genetics and genetic dissection of heritable diseases and detection of associated mutations and diagnostics based on PCR.
3. Technologies being adapted for further applications like closing of animal with a capacity to produce human macromolecules.

 

IV Bio BC 114- Dissertation/Project work

The project work will involve in depth practical work on a problem suggested by the supervisor of the candidate. The student will submit the dissertation of the work done. The dissertation submitted by the candidate shall be evaluated by one external expert, head of the department and supervisor of the candidate. The seminars, in – plant training and industrial visit reports will also be submitted by the candidate to the Head of the Department who will submit these to the external examiner. The examination shall be held in the department and the dissertation etc. will NOT be required to be mailed to the external examiner. The distribution of marks will be as under.