Bioche Syllabus PDF

1 M.
Sc BIOCHEMISTRY SYLLABUS FOR THE ACADEMIC YEAR 2017-19 (APPROVED BY BOS MEMBERS)
07-08-2017
RAYALASEEMA UNIVERSITY::KURNOOL
M.Sc BIOCHEMISTRY (SEMESTER SYSTEM)
(Syllabus w.e.f. academic year 2017-18)
Semester Title of the Paper Credits Max. Min.

marks marks
Theory
I - Cell Biology (Common) 4 100 35
II - Basic Microbiology (Common) 4 100 35
III - Biomolecules – Structure and Function 4 100 35
(Common)
IV - Immunology 4 100 35
I
Practicals
I - Cell Biology (Common) 2 50 18
II - Introduction to Microbiology (Common) 2 50 18
III - Biomolecules – Structure and Function 2 50 18
(Common)
IV - Immunology 2 50 18
Total Credits: 24C – Theory – 16C; Practicals – 08C
Total marks – 600 (400+50+50+50+50)
Marks allocation for theory examinations:
Max. Marks 100 – Theory main exam - 70M
Internal Assessment - 20M
Seminar - 10 M
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2 M.Sc BIOCHEMISTRY SYLLABUS FOR THE ACADEMIC YEAR 2017-19 (APPROVED BY BOS MEMBERS)
07-08-2017
SEMESTER I
PAPER I – CELL BIOLOGY (Common)
Objectives:
On completion of this course the student will be able to
1). Understand the basic cell types, cell organelles ‘types and their functions
2). Understand the cell signaling molecules and their function
3). Understand the mechanism of cell division of plant and animal cells
4). Understand the cancer development and apoptosis
Specific objective:
Students will know the molecular structure and functions of cell organelles and signaling
molecules involved in the apoptosis and development of cancer.
Credits - 4
Unit–I: Cells, cell types, Cellular organelles: Cell organelles and their structural organization:
Prokaryotes and Eukaryotes, Plasma membrane, Chloroplasts; Mitochondria; Golgi complex;
Endoplasmic reticulum; Vacuole; Nucleus and Nucleolus; Functional domains within the
Nucleus; Nucleolus; Micro bodies; Lysosomes; Structure and function of plant cell wall. Germ
cells, Somatic cells: Muscle, liver, neuronal and glial cells.
Unit –II: Nomenclature of chromosome; C-value paradox; Organization of Eukaryotic

chromosome; Structure of Nucleosome; Euchromatin and Hetero chromatin; Cytoskeleton -
Structure and Organization of cytoskeletal filaments - Actin and Intermediate filaments;
Microtubules. Microtubule motors and movement and Nucleation.
Unit- III: Cell Communication: Cell surface receptors and Intracellular receptors; Intracellular
signaling - Autocrine, Paracrine, Contact dependent, Synaptic and Endocrine signaling;
Response of cell to signals; Cell surface receptors - Ion channel linked, G- protein linked and
Enzyme linked receptors; Intracellular signaling proteins - Different types and their role;
Second messengers; cAMP pathway and role of calcium; Cellular interactions: Microvilli, Tight
junctions, Belt and Spot Desmosomes. Gap junctions - Electrical coupling, the connexon.
Permeability to ions and small molecules. Factor mediating cell-self recognition, Cellular
interaction Cyclic AMP and cyclic GMP.
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Unit IV: Cell cycle - Overview of eukaryotic cell cycle, Regulation of cell cycle by cell growth
and extra cellular signals, Cell cycle check points, Regulation of cell cycle progression - Protein
kinases; MPF; Cyclins and Cyclin dependent kinases. Cell Death: i) Apoptosis - Definition,
Morphological and Biochemical differences between Apoptosis and Necrosis; Mechanism
(Intrinsic pathway and Extrinsic pathway), Inhibitors of Apoptosis and Significance. ii) Cancer
Development and causes of Cancer; Properties of Cancer cells; Approaches to Cancer treatment.
List of Practicals: (Cell Biology)
1. Preparation of Cytological slides for Mitosis using Root tips.

2. Preparation of Cytological slides for Meiosis-I using Flower buds; Chiasma Frequency.
3. Identification of different stages of Mitosis and Meiosis.
4. Demonstration of Chromosomal (Structural and Numerical) Aberrations.
5. Isolation of cell organelles.
6. Isolation of Chloroplast
7. Isolation of Mitochondrial fraction by differential gradient centrifuge
Outcome of the course:
Students will understand the different types of cells, cell divisions, signaling molecules
involved in cell communication and growth and development of cancer
Suggested Readings: (Cell Biology)

1. Cooper Geoffrey, M. - The Cell-A Molecular Approach, ASM Press, Washington.
2. Sharma, A.K & A. Sharma. - Chromosome Techniques: Theory & Practice, Batter
Worth.
3. Albert’s, A. et al. - Molecular Biology of the Cell, Garland Publishing House, New York.
4. De Robertis, E.D.P. & E.M.F. DeRobertis. - Cell and Molecular Biology, Lippincott
Williams & Wilkins, Bombay.
5. Powar, C.B. - Cell Biology.
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SEMESTER I
PAPER II – BASIC MICROBIOLOGY (Common)
Objectives: On completion of this course the student will be able to
Understand the taxonomy and of classification of microbes.

Study the structure and function of Bacterial cell.
Study the nutritional mechanisms and growth kinetics of microbes
Study the interactions, pathogenesis and diseases caused by microbes.
Study the industrial applications of microbes
Credits - 4
Unit – I
History and scope of Microbiology. Recent trends and developments in modern microbiology.
Identification, characterization and classification of microorganisms, Principles of bacterial
taxonomy and classification: - Bergy’s manual and its importance, Concepts, nomenclature and
taxonomic ranks: Major characteristics used in Taxonomy - morphological, physiological and
metabolic, ecological, numerical taxonomy, genetic and molecular classification systems; the
kingdoms of organisms and phylogenetic trees. Distinguishing characteristics between
prokaryotic and eukaryotic cells, Structure and function of Cell wall of bacteria, cell membranes,
flagella, pili, capsule, gas vesicles, carboxysomes and magnetosomes.
Unit – II
Microbial nutrition - common nutrient requirements, Nutritional types of microorganisms,
Bacterial growth Dynamics. Microbial growth - Requirements for growth. Bacterial Adaptations,
Extremophiles (Acidophiles, Alkaliphiles, Thermophiles, Halophiles, Psychrophiles). Control of
Microorganisms by Physical and Chemical Agents. Structure and classification of viruses,
viroids and prions; Modern concepts in virology: Replication, Assembly, Mode of infection,
Transduction.
Unit – III
Pathogenicity of Microorganisms – Host – Parasite relationships, Pathogenicity of Viral diseases
- Entry, Contact, and Primary Replication, Viral Spread and Cell Tropism, Host Immune
Response, Recovery from Infection, Virus Shedding. Pathogenesis of Bacterial Diseases -
Maintaining a Reservoir of the Bacterial Pathogen, Transport of the Bacterial Pathogen to the
Host, Attachment and Colonization by the Bacterial Pathogen, Invasion of the Bacterial
Pathogen, Growth and Multiplication of the Bacterial Pathogen, Leaving the Host. Human
Diseases Caused by Viruses, Prions; Bacteria and Fungi. Biofilm formation.
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Unit – IV
Application of Microorganisms in Industry - choosing microorganisms for industrial
microbiology and biotechnology, Finding Microorganisms in Nature, Genetic Manipulation of
Microorganisms, Preservation of Microorganisms. Major Products of Industrial Microbiology -
Antibiotics, Amino Acids, Organic Acids, Biopolymers, Biosurfactants, Bioconversion
Processes. Acetone-butanol-ethanol (ABE) Fermentation. Microbiology of Fermented Foods -
Yogurt, Cheese Production, Meat and Fish, Production of Alcoholic Beverages and Breads.
Probiotics.
List of Practicals: (Basic Microbiology)

1. Isolation of Pure Cultures
2. Serial Dilution
3. Growth measurement by using spectrophotometer
4. Calculation of cell number from OD Units
5. Determination of Doubling time
6. Gram staining
7. Yeast Fermentation process
8. Influence of temperature, pH and salt on growth of bacteria
Outcome:
The students will be able to identify and classify microbes based on Bergy’s manual.
The students will be able to describe the structure & function of Bacteria.
The students will be able to describe how the nutritional uptake and growth of microbes
occurs by controlling physical and chemical agents.
The students can able to understand the detailed structure & classification of viruses &
also how the replication & assembly of virus occurs.
The students will be able to understand pathogenicity of microorganisms (parasites,
virus) and can identify human diseases caused by Bacteria, Fungi, Viruses and prions.
The students will be able to know the application of microorganisms in industry e.g:
Antibiotics, Amino Acids, etc.
The students will be able to understand different processes in microbiology of fermented
foods.
Suggested Readings: (Basic Microbiology)

1. MJ. Peleczar, Jr & E.C.S Chan International students - Elements of Microbiology,
McGraw Hill International Book Company, New Delhi.
2. C.B. Powar & H.F. Daginawala - General Microbiology, Himalaya Publishing House,
Bombay.
3. R Aananthnarayan & C.K. Jayaram Panikar - Text Book of Microbiology, Orient
Longmen, Hyderabad.
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4. A. Mani, A. M. Selvaraj, L.M. Narayanan and N. Arumugam – Microbiology, Saras

Publications.
5. Bauman Robertt et al. – Microbiology with diseases: Taxanomy, Benjamin Cummings
Publishers.
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SEMESTER I
PAPER III – BIOMOLECULES: STRUCTURE AND FUNCTION (Common)
Credits – 4
Learning Objectives
 To learn about fundamentals of Chemical foundations of Biology.

 To learn about Structural and Functional aspects of Biomolecules like Carbohydrates,
Protein, lipids and Nucleic acids etc.
Unit – I
Chemical foundations of biology: Chemical bonds, pH, pKa, acids, bases, buffers, isomerism.
Principles and Laws of thermodynamics, Properties of water.
Carbohydrates: Definition, classification, stereo isomeric forms, structure, functions and
reactions of biologically important carbohydrates viz. Monosaccharide - glucose, fructose,
mannose, galactose, arabinose; Disaccharides – sucrose, lactose, maltose, cellobiose; structural
and storage polysaccharides- starch, glycogen, inulin, hemicelluloses, cellulose, lignin, chitin and
peptidoglycans.
Unit – II
Amino acid, peptide and proteins: Amino acids: Classification, Properties, reactions, rare
amino acids; Biologically important peptides; Protein classification: Reactions, functions,
properties and Solid phase synthesis; Structural levels of protein: (a). Primary Structure: Peptide
bond, importance of primary structure. (b). Secondary structure: alpha-helix, β - structure, β-
helix, super secondary structure. (c). Tertiary Structure: Forces stabilizing, unfolding/ refolding
experiments. Prediction of tertiary Structure (d). Quaternary structure – haemoglobin; End group
analysis, sequencing and peptide synthesis, Ramachandran plot and its significance.
Unit – III
Lipids and Fatty acids: Definition and nomenclature, Fatty acids and their types, structure and
biological functions of various class of lipids – Triacyl glycerol, phospholipids, glycolipids,
sphingolipids, terpenoid lipids, including steroids, alkyl glyceryl ethers and wax;
Lipoproteins; Lipids of physiological significance; Lipid transport and storage; Bio- membranes;
formation of micelles; bilayers, vesicles, membrane composition and fluid mosaic model.
Structure and functions of Polyamines, Prostaglandins, Thromboxanes, leucotrienes. Types and
functions of Porphyrins, pigments and growth regulators.
Unit – IV
Nucleic acids: Building blocks of nucleic acids- purines and pyrimidines, nucleosides,
nucleotides; Types of DNA (A, B and Z); Double stranded linear DNA; Circular DNA and Extra
chromosomal DNA; Watson and Crick DNA double helix model; Chargaff’s rule; DNA
organization, Stability and formation of phosphodiester linkages; Effect of acids, alkali and
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nucleases; Supercoiling, helix to random coil transition; denaturation of nucleic acids and
melting temperature; Different types of RNA and their biological functions.
List of Practicals: (Biomolecules – Structure and Function)
1. Determination of reducing sugars by spectrophotometer
2. Identification of amino acids by paper chromatography
3. Analyzing of amino acids by TLC
4. Isolation of Protein
5. Estimation of Proteins
6. Separation of Proteins by SDS PAGE
7. Isolation of lipids
Course Outcome:
Students should understand the both structural and Functional aspects of biologically
important molecules. It should pave a path to learn about the metabolic pathways of biologically
important molecules and their biomedical significance. Students should apply their knowledge
towards research
Suggested Readings: (Biomolecules – Structure and Function)

1. Lehninger- Principles of biochemistry by Nelson D. Cox Michael M - 6th Edition
2. Biochemistry by L. Stryer - 4th Edition
3. Biochemistry by V.Voet and J.G.Voet - 4th Edition
4. Harpers Illustrated Biochemistry by Victor W. Rodwell, David Bender, Kathleen M.
Botham - 30th Edition
5. Modern Experimental Biochemistry by Rodney F. Boyer - 3rd Edition
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SEMESTER I
PAPER IV – IMMUNOLOGY
Objectives:
 To study the structure and function of immune system.

 To identify the blood grouping and their function.
 To study the antibody and antigen interaction.
 To investigate the diseases pathogenesis and treatment.
 To study the different kind of Hypersensitivity reactions.
Credits - 4
Unit – I
Introduction: Origin of immune system - History of immunology - Types of immunity,
characteristics of innate and acquired immunity; Antigens: Types of Antigens - general
properties; adjuvants; antigenic determinants or epitopes; generation of B-cell and T-cell
receptors; Antibodies (Immunoglobulins): Basic structure, properties, isotypes, allotypes and
idiotypes; Classes of immunoglobulins - functions in relation to their structure; Organization and
expression of immunoglobulin genes.
Unit – II
Cells of immune system: Types and structure of lymphocytes - T and B lymphocytes, Null cells,
NK cells, lymphocytic traffic; T and B cell generation, activation and differentiation; Lymphoid
organs: Organs of immune system - primary and secondary lymphoid tissues; Immune response:
Cell mediated and Humoral immunity - Factors influencing antibody formation, Immunological
memory, Differences between primary and secondary immune responses.
Unit – III
Antigen and antibody interactions: Forces involved in antigen antibody binding - antigen
antibody binding sites, antibody avidity, cross reaction, bonus effect; Antigen – antibody
interactions – precipitation, agglutination, opsonization, flocculation reactions; Complements
and Major Histocompatibility Complex : Salient features of complements, biosynthesis of
complements, pathways of complement activation; Types and structure of MHC molecules and
antigen presentation; Hybridoma Technology, Monoclonal and Polyclonal antibody production.
Introduction of Autoimmuno disorders and immune response to infectious diseases.
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Unit – IV
Hypersensitivity: Factors causing hypersensitivity - Types and their characteristic reaction with
specific examples; Immunohaematology: ABO blood group system - Distribution and
transfusion - Rh blood group system - application of blood groups; Immunodeficiency and
AIDS; Vaccines and its types.
List of Practicals: (Immunology)

1. Antigen – Antibody interaction in vitro (Blood grouping)
2. Isolation of B-lymphocytes
3. Separation of serum protein
4. Histology of lymphoid organs
5. Immunological tests: Immunodiffusion and Immunoelectrophoresis.
Outcome:
 Will be able to identify the cellular and molecular basis of immune responsiveness.
 Will be able to describe the roles of the immune system in both maintaining health and
contributing to disease.
 Will be able to describe immunological response and how it is triggered and regulated.
Suggested Readings: (Immunology)

1. Kuby, J. (1998) Immunology, W.H. Freeman and Company, New York.
2. Essentials of Immunology by Ivan M.Roitt.
3. An introduction of Immunology by C.V. Rao
4. Immunology by Dulsy Fatima and Armugam
5. General Immunology by E.L. Cooper
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marks marks
Theory
I - Genetics and Evolution (Common) 4 100 35
II - Enzymology (Common) 4 100 35
III - Tools and Techniques in Biology 4 100 35
(Common)
IV - Bioenergetics and Intermediary 4 100 35
Metabolism
II
Practicals
I - Genetics and Evolution (Common) 2 50 18
II - Enzymology (Common) 2 50 18
III - Tools and Techniques in Biology 2 50 18
(Common)
IV - Bioenergetics and Intermediary 2 50 18
Metabolism
Total marks – 600 (400+50+50+50+50)
Seminar - 10 M
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SEMESTER II
PAPER I – GENETICS AND EVOULTION (Common)
Objectives:
o To study the Mendel principles of Genetics and Genetic Recombination.

o To know the Chromosome as a Linkage unit, Chromosomal Mapping, Chromosomal
Aberrations, Sex- linked inheritance
o To study the Structural abnormalities of Human chromosomes and Syndromes
Concepts of Eugenics and genetic counseling
o To study about principles of evolution and Darwinism ,Neo-Darwinism and Lamarckism.
Credits - 4
Unit – I
Mendelian Laws of Inheritance: An Overview: Genetic conventions, Notations and Terminology.
Genetic Recombination: Types (Homologous - Reciprocal and Non-reciprocal, Site specific and
Illegitimate). Different models of Homologous Recombination. Molecular Mechanisms of
Recombination. Non-Mendelian inheritance.
Unit – II
Chromosome as a Linkage unit: Coefficient of Coincidence of Double Crosses, Chiasma
Interference. Chromosomal Mapping: Mapping by Recombinational Frequencies,
Transformation and Interrupted Mating. Chromosomal Aberrations: Types (Numerical and
Structural) and their significance in Evolution.Sex Chromosomes: Determination of Sex; Genic
balance theory;Gynandromorphs; Sex- linked inheritance; Criss - cross inheritance.
Unit – III
Numerical (aneuploidy: trisomy, monosomy, nullisomy; euploidy) and Structural abnormalities
(deletion, duplication, inversion and translocation) of Human chromosomes and Syndromes:
Turner’s; Down’s and Klinifelter.Human karyotype and Human genome. Inborn errors of
Metabolism.Pedigree analysis. Concepts of Eugenics: Artificial Insemination, sperm banks,
Amniocentesis, Consanguinity, prenatal diagnosis. Inborn diseases and genetic counselling.
Unit – IV
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Emphasis on Darwinism and Lamarckism.Neo-Darwinism.An account on destabilizing forces:

(i) Natural selection (ii) Mutation (iii) Genetic drift. Hardy and Weinberg equilibrium and its
significance in understanding Evolution.Modes of Speciation: (Allopatric, Sympatric and
Parapatric). Phylogenetic Gradualism and Punctuated Equilibrium.Micro and Macro Evolution.
List of Practicals: (Genetics and Evolution)

1. Mendelian Laws using Colour Marbles or Beads.
2. Evaluation of Segregation and Random assessment using Chi-Square test or Test of
fitness.
3. Demonstration of Barr bodies.
4. Construction of Genetic Maps based on problems in two and three factor crosses.
5. Demonstration of Neo-Darwinism and Lamarckism.
6. Charts – Micro and Macro Evolution.
7. Sex determination of Drosophila
8. Culturing drosophila using standard methods
9. Variance of eye and wings studies in drosophila
Outcome:
 The students will be able to differentiate different models in Homologous recombination.

 The students will be able to know Chromosomal Mapping, Chromosomal Aberrations,
Genic balance theory.
 The students will be able to know Numerical & Structural abnormalities of Human
chromosomes and Syndromes, Concepts of Eugenics Inborn diseases and Genetic
Counseling.
 The students will be able to know Emphasis on Darwinism ,Neo-Darwinism &
destabilizing forces
Suggested Readings: (Genetics and Evolution)

1. B. D. Singh, P.B. KaviKishor, PratibhaNallari, P. H. Rao. Cell Biology and Genetics;
Genetics : Fundamentals.Kalyani Publishers, Hyderabad, New Delhi. Published in the
year2009.
2. Monrve W. Strickberger – Genetics.
3. K.B. Ahluwallia - Genetics.
4. E.J. Gardner. M.J. Simmons and D.P. Snustad- Principles of Genetics.
5. Watson, J.D., N.H. Hopkins, J.W. Roberts, J.A. Steitz and A.M. Weiner - Molecular
Biology of Genes, Benjamin Cummings Publishing Company. Inc. Tokyo.
6. E.J. Mange, Arthur P. Mange - Basic Human Genetics, Indian Print.
7. M.R. Goodman - Genetic disorders of Man.
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SEMESTER II
PAPER II – Enzymology (Common)
Objectives:
 To study the basic knowledge of enzymes, know the parameters of the enzymatic
reaction.
 To learn the mechanisms of action of enzymes and inhibitors.

 To learn the knowledge of the structure of enzymes and amino acids that builds active
sites of enzymes.
 To introduce students to various theoretical and practical aspects of enzymology.
Credits - 4
Unit - I
Nomenclature and classification of enzymes: EC, Vitamin cofactors: TPP, FMN/FAD,
NAD/NADP, Pantothenic acid; Factors affecting catalysis (pH, temperature, pressure, enzyme
and substrate concentration); Chemicals to identify active site residues: Arg, Cys, Lys, His.
Unit - II
Kinetics of catalysed reaction: Single substrate reactions, bisubstrate reactions (ordered, random,
sequential, Ping-Pong), Michaelis-Menton kinetics (derive equation and transformations);
Transformation of Michaelis-Menton equation, Determination and significance of kinetic
constants, Activation energy and Arrhenius concept. Enzymes activation by ligand binding and
dimerization (protein tyrosine kinase receptors). Reversible and irreversible activation of
enzymes (pro-enzymes, phosphorylation). Inhibitors (competitive, uncompetitive,
noncompetitive, suicide). Enzyme inhibitors as drugs: RT and Protease inhibitors as anti-HIV
drugs
Unit - III
Enzyme catalysis: enzyme specificity and the concept of active site, determination of active site.
Stereospecificity of enzymes. Mechanism of catalysis: Proximity and orientation effects, general
acid-base catalysis, concerted acid - base catalysis, nucleophilic and electrophilic attacks,
catalysis by distortion, metal ion catalysis. Catalytic mechanism of RNase, Chymotrypsin,
Trypsin, Lysozyme, Carboxypeptidase and Subtilisin.
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Unit - IV
Enzyme regulation: General mechanisms of enzyme regulation. Regulation of Glutamine
Synthetase. Allosteric regulation of Aspartate Transcarbamylase. Sigmoidal kinetics and their
physiological significance, Symmetric and sequential modes for action of allosteric enzymes.
Multi-enzyme Complex: fatty acid synthase. Cooperativity in binding (oxygen binding to
hemoglobin). Cooperativity: MWC model, KNF model. Immobilised enzymes and their
industrial applications. Isoenzymes and their significance.
List of Practicals: (Enzymology)
1. Assay of Amylase from saliva
2. Assay of Acid phosphatase from potato
3. Assay of Trypsin
4. Assay of urease from Horse gram
5. Assay of Succinate dehydrogenase from the liver
6. Effect of temperature on enzyme activity and calculation of energy of activation.
7. Enzyme kinetics
8. Effect of PH on enzyme activity and determination of optimum PH
9. Effect of substrate concentration on enzyme activity and determination of Michealis
constant.
Outcome:
 The students will be able to differentiate different models in Homologous recombination.

 The students will be able to know Chromosomal Mapping, Chromosomal Aberrations,
Genic balance theory.
 The students will be able to know Numerical & Structural abnormalities of Human
chromosomes and Syndromes, Concepts of Eugenics Inborn diseases and Genetic
Counseling.
 The students will be able to know Emphasis on Darwinism ,Neo-Darwinism &
destabilizing forces
Suggested Readings: (Enzymology)

1. Lehninger Principles of Biochemistry, David L. Nelson, Michael M. Cox Publisher: W.
H. Freeman.
2. Molecular Biology of the Cell, 3rd edition. Bruce Alberts, Dennis Bray, Julian Lewis,
Martin Raff, Keith Roberts, and James D Watson. Publisher New York: Garland Science.
3. The Cell: A Molecular Approach, Fifth Edition, by Geoffrey M. Cooper and
Robert E. Hausman, published by ASM Press.
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SEMESTER II
PAPER III – TOOLS AND TECHNIQUES IN BIOLOGY (Common)
Objectives:
 To understand the principles and applications of Microscopy
 To understand the principles and applications of Chromatography
 To understand the principles and applications of Electrophoresis
 To understand the principles and applications of Spectroscopy
Credits - 4
Unit -I
Microscopy and Centrifugation: Principles and application of light, phase contrast, fluorescence,
scanning and transmission electron microscopy. Microtomy and double staining of plant
sections. Centrifugation: Basic principles of sedimentation, types of centrifuges and rotors.
Centrifugation methods: differential, density-gradient, analytical, and ultracentrifugation and
their applications.
Unit-II
Chromatography: Separation methods - General principles and applications. Affinity, Gel
filtration, Ion exchange, Partition and adsorption chromatography. Techniques of paper
chromatography, Thin layer chromatography, Gas and High performance liquid chromatography.
Unit -III
Electrophoresis: General principles and applications. PAGE: Native -PAGE, SDS-PAGE,
Isoelectricfocusing, 2D electrophoresis, identification of proteins in 2D gels, capillary
electrophoresis. Agarose gel electrophoresis –Preparation of gel and separation of DNA and
RNA, Elution of DNA from agarose gels. Hybridization, Electrophoretic mobility shift assay
[EMSA].
Unit - IV
Spectroscopy and Radioisotope techniques: Principles, laws of light absorption, Instrumentation
and applications of UV- visible spectrophotometer, fluorescence spectroscopy, Mass
spectroscopy – Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI –
TOF). Radioisotope Techniques: Types of isotopes, radioactive decay. Detection and
measurement of radioactivity. GM counter, scintillation counter, autoradiography. Isotopes used
in biology, safety methods in handling radioisotopes.
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List of Practicals: (Tools and Techniques in Biology)

1. Determination of Wavelength of Maximum Absorbance
2. Separation of Biological compounds by Paper chromatography
3. Determination of Tm value of DNA
4. Determination of molecular extinction coefficient
5. TLC analysis for amino acids
6. Western blot analysis.
7. Preparation of Buffers and measurement of pH
Outcomes of the course:

After completion of the course tools and techniques in Biology, the students will understand
how the techniques are useful to understand the molecular structure of the
plant/animal/microbial cell structures. They will understand the separation of biological
molecules by using different techniques.
Suggested Readings: (Tools and Techniques in Biology)

1. Ed.John. R.W.Masters - Animal Cell culture: A Practical approach, IRL Press.
2. Ronert Braun - Introduction TO Instrumental Analysis, McGraw Hill International.
3. K. Wilson & K.W. Goulding - A Biologists Guide to Principles and Techniques of
Practical Biochemistry, ELBS Edn.
4. K.T. Brown and D.G. Flamming IBRO - Advanced Micropipette Techniques for cell
physiology Hand Book Series, A Wiley Interscience publications, John Wiley and Sons,
New York.
5. N.J. Stransfed and T.A. Miller - Neuro anatomical Techniques, Springer Verlag, New
York Heidelberg, Berlin.
6. Robert S. Feldman, Jerrold S. Meyer and Unida quenzer - Principles of
Neuropsychopharmacology, Sinancer Associates Inc. Publishers. Sunderland,
Massachusetts.
7. F.M. Weesner - General Zoological Microtechnique
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SEMESTER II
PAPER IV – BIOENERGETICS AND INTERMEDIARY METABOLISM
Objectives:
Bioenergetics:
 Discuss the importance of order (organization) to living systems.
 Explain the concept of energy, cite examples and assess its importance to living
organisms.
 Restate the two Laws of Thermodynamics.

 Relate the concept of entropy to the Laws of Thermodynamics.
 Define free energy and discuss its relationship to chemical equilibria.
Credits - 4
Unit – I
Concept of free energy, standard free energy, determination of ∆G for a reaction.
Relationship between equilibrium constant and standard free energy change, biological standard
state & standard free energy change in coupled reactions. Laws of Thermodynamics, relevance
of entropy and enthalpy in biological systems and reactions – first and second order reactions.
Unit – II
Digestion and absorption of carbohydrates. Glycolysis and its regulation. Substrate cycling,
Glycogen metabolism and its regulation with special reference to phosphorylase and glycogen
synthase. TCA cycle – function and regulation, Pyruvate dehydrogenase complex, Glyoxylate
cycle, Cori’s cycle. Pentose phosphate pathway. Gluconeogenesis and its regulation. HMP shunt
(Pentose phosphate pathway) and its significance, Uronic acid pathway. Regulation of blood
glucose homeostasis. Metabolism of fructose, galactose and lactose. Hormonal regulation of
carbohydrate metabolism.
Unit – III
Oxidation of fatty acids- mitochondrial and peroxisomal β - oxidation, oxidation of unsaturated
and odd chain fatty acids, ketone bodies. Fatty acid synthesis, desaturase and elongase. Lipid
biosynthesis- biosynthesis of Triglycerides, phosphoglycerides and sphingolopids. Ketone
bodies- formation and utilization.
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Unit – IV
General reactions of protein metabolism, essential amino acids. General reactions of amino acid
metabolism - Transamination, decarboxylation, oxidative & non-oxidative deamination of amino
acids. Special metabolism of methionine, histidine, tyrosine, lysine, valine, isoleucine and
polyamines. Urea cycle and its regulation. Inborn errors of protein metabolism.
Biosynthesis of purines and pyrimidines - De novo and salvage pathways and their regulation.
Catabolism of purines and pyrimidines. Biosynthesis of ribonucleotides and
deoxyribonucleotides. Inherited disorders of purine and pyrimidine metabolism.
List of Practicals: (Bioenergetics and Intermediary Metabolism)

1. Measurement of Oxygen from mitochondria.
2. Estimation of oxygen from aquatic organisms using oxygraph.
3. Quantification of NAD+/NADP+ using UV visible method
4. Hemoglobin estimation
Outcome:
 Learn importance of thermodynamics in living systems.
 Explore the consequences of energy, thermodynamics laws and significant of chemical

equilibrium in living systems.
Suggested Readings: (Bioenergetics and Intermediary Metabolism I&II)

1. Principles of Biochemistry - L. Stryer (W.H. Freeman & Co.).
2. Principles of Biochemistry - A.L.Lehninger, D.W.Nelson & M.M.Cox (Macmillan).
3. Biochemistry - D.Voet & J.G.Voet (John Willey).
4. Harper’s Illustrated Biochemistry - R.K.Murray et al. (McGraw Hill).
19
07-08-2017

marks marks
Theory
I. Molecular Biology (Common) 4 100 35
II. Biometry/Biostatistics/Bioinformatics 4 100 35
(Common)
III. Nutrition and Clinical Biochemistry 4 100 35
IV. Endocrinology, Developmental Biology and 4 100 35
Physiology
III
Practicals
I. Molecular Biology (Common) 2 50 18
II. Biometry/Biostatistics/Bioinformatics 2 50 18
(Common)
III. Nutrition and Clinical Biochemistry 2 50 18
IV. Endocrinology, Developmental Biology and 2 50 18
Physiology
Total marks – 600 (400+50+50+50+50)
Seminar - 10 M
20
07-08-2017
SEMESTER III
PAPER I – MOLECULAR BIOLOGY (Common)
On completion of this paper/module, you will be able to -
1. Name the major proteins and enzymes along with their functions involved in DNA
Replication process.
2. List the different factors responsible for DNA damage and can explain different
methods/enzymes involved in DNA Repair.
3. Explain what is Transcription? Explain in detail about the various components and
different steps in the process of Transcription. Importance of Post-Transcriptional
Modifications.
4. Explain what is meant by the ‘genetic code’ and how it relates to protein synthesis.
Explain in detail about the steps in Protein synthesis and the importance of Post-
Translational Modifications. Sorting and Targeting of different proteins in the cells.
5. Define Antibiotic and Inhibitor. Explain the importance of antibiotics in the treatment of
diseases. Explain the antibiotics mechanism of actions (on protein synthesis) affecting the
growth of pathogenic microorganisms.
6. Understand what Gene expression is and how the genes are regulated. Explain the
arrangement of genes in prokaryotes and eukaryotes. Importance of lac operon and ara
operon.
7. Importance of Antisense RNA technology.
8. Explain various factors affecting gene expression such as environmental and hormonal.
Importance of gene expression during development (Homeotic genes) and how those
genes are regulated.
Credits - 4
Unit - I
DNA as genetic materials – Experimental evidences: Organization of DNA in prokaryotes and
Eukaryotes. DNA Replication and Repair - Modes of Replication, Experimental evidences for
Semi Conservative mode of Replication – Messelson - Stahl and Cairns experiments; Replication
21
07-08-2017
fork, Continuous and Discontinuous DNA synthesis; Enzymes and Proteins in Replication -
Single Strand DNA binding Proteins (SSB), Helicases, Topoisomerases, DNA Ligases; Priming
by RNA Polymerase and Primase; DNA Polymerases - E.coli DNA Polymerase I, II and III and
Eukaryotic DNA Polymerases. DNA Damage and repair mechanisms.
Unit - II
Transcription: Polynucleotide phosphorylase, RNA polymerases - Structure of E.coli RNA
polymerase; sigma factor, sigma cycle, Promoter-polymerase interaction. Nature of Eukaryotic
RNA polymerases; Enhancers, Initiation, Elongation and Termination of RNA Synthesis.
Processing of RNA (Capping, Splicing, Tailing).
Unit - III
Translation (Protein synthesis) - Mechanism of Initiation, Elongation and Termination of Protein
synthesis; Inhibitors of Protein synthesis; Post-Translational Modifications; Protein sorting and
Targeting.
Unit - IV
Regulation of Gene Expression - House Keeping genes, Constitutive and Regulatory genes;
Inducers and Repressors; Regulation of Gene expression in Prokaryotic Operons - Negative
regulation and Positive regulation; Fine structure of lac operon - Repressor and the Catabolite
activator proteins in gene regulation of lac operon; Dual functions of the Repressor in ara
operon; Antisense RNA; Hormones and Environmental factors affecting Gene expression;
Homeotic genes and their Regulation. siRNA and miRNA- RNA interference.
22
07-08-2017
List of Practicals: (Molecular Biology)

1. Isolation of DNA from bacterial, plant and animal cells.
2. Estimation of DNA by Diphenylamine methods
3. Estimation of RNA by Orcinol method.
4. Determination of purity and quantity of DNA by UV absorption method.
5. Determination of GC content of DNA and estimation by Tm
Suggested Readings: (Molecular Biology)

1. B. Alberts, D. Bray, J.Lewis, M.Raff, K. Roberts and J.D.Watson - Molecular Biology of
the Cell, Garald Publishing, New York & London.
2. D. Freifelder - Molecular Biology – A Comprehensive Introduction to Prokaryotes and
Eukaryotes, Jones and Bartlett, USA.
3. Maniatis, E.F.Fritsch and J.Sambrook - Molecular Cloning: Laboratory Manual, Cold
Spring Harber Laboratory, NewYork.
4. Benjamin Lewin – Genes, Oxford University Press.
5. Nelson and Cox - Principles of Biochemistry.
6. Alberts Johnson et al. – Molecular Biology of the Cell, Garland Science, New York.
23
07-08-2017
SEMESTER III
PAPER II – BIOMETRY, BIOSTATISTICS AND BIOINFORMATICS (Common)
Objectives:
 To make proper use of raw data.

 To make the study of data and comparison easier.
 To put up the collected material to statistical treatment.
 To simplify the complexities of raw data and make it possible to draw statistical
inferences.
 To read the analysis of gene and protein sequences to reveal protein evolution and
alternative splicing, the development of computational approaches to study and predict
protein structure to further understanding of function, the analysis of mass spectrometry
data.
 To study the development of computational methods to utilize expression data to reverse

engineer gene networks in order to more completely model cellular biology.
 To study of population genetics and its connection to human disease.
Credits - 4
Unit – I
Data – Data types, Collection of data, Classification and Tabulation. Measures of Central
tendencies – Mean, Median and Mode. Measures of Variation – Range, Quartile deviation, Mean
deviation and Standard deviation. Coefficient of variation. Probability – Addition and
Multiplication theories, Conditional probability and Probability distributors – Binomial, Poisson
and Normal distribution.
Unit – II
Correlation and Linear Regression – Scatter diagram method – Karnal Pearson’s Rank
correlation methods. Regression lines– Fitting of regression lines by least squares method –
Regression coefficients and properties. Small tests – t, F and chi square tests. ANOVA – one
way and two way classification. Duncan’s Neuman-Keuls multiple range (DMR) tests.
Unit – III
Introduction to bioinformatics- Biological Databases and their importance. Primary and
Secondary protein and nucleic acid Databases. Genomic and Proteomic Pathway Databases.
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Overview of primary, secondary structural elements. Protein secondary prediction, Introduction

to molecular modeling concepts and applications.
Unit – IV
Sequence Analysis – Sequence Alignments methods- Dot plots, pair wise and multiple sequence
alignments. Global Vs Local Alignment, Dynamic programming- PAM and BLOSUM scoring
matrices-Homolog, Paralog and ortholog. Domine and Motifs, Patterns and profiles.
Phylogenetic studies, Dendrograms, Phylograms, Cladograms.
List of Practicals: (Biometry, Biostatistics and Bioinformatics)

1. Downloading genes and EST sequences from databases.
2. Sequence alignment - pair wise and multiple sequences.
3. Primer designing.
4. Phylogenetic analysis at the nucleotide and amino acid sequence levels. Construction of
phylogenetic trees using software tools.
5. Genome sequence analysis for the identification of coding gene sequences.
6. Identification of promoter sequences in the genome sequences.
7. Chi-test
8. ANOVA
Outcomes:
 Apply basic statistical concepts commonly used in health sciences.
 Use basic analytical techniques to generate results.
 Interpret results of commonly used statistical analyses in written summaries.
 Demonstrate statistical reasoning skills correctly and contextually.
Knowledge and awareness of the basic principles and concepts of biology, computer science and
mathematics
Suggested Readings: (Biometry, Biostatistics and Bioinformatics)
1. P.B. Kavi Kishor and L.N. Chavali. Principles of Biological Databases. Himalaya
Publishing House, Hyderabad, New Delhi, Chennai, Mumbai. Published in 2013.
2. Sokal – Rohlf - Introduction to Biostatistics (2nd Edn.), Freeman International Edition.
3. Goldstein, A - Biostatistics – An Introductory text, The McMillan Co., New York.
4. Lewis Alvin E. - Biostatistics, Affiliated East – West Press Pvt., Ltd., New Delhi.
5. Bailey Norman T.J. - Statistical Methods in Biology, The English Language Book
Society & The English University Press Ltd.
6. Holdan Bancroft - Introduction to Biostatistics, Paul B. Hoebar Inc., New York.
25
07-08-2017
SEMESTER III
PAPER III – NUTRITION AND CLINICAL BIOCHEMISTRY
Objectives:
 To enhance knowledge of nutrition and metabolism and the application of such

knowledge to the maintenance of health and the treatment of disease.
 To provide an organization which encompasses the needs of professionals from all

disciplines with a common interest in nutrition.
 To develop a detailed awareness of specific clinical biochemistry topics studying from

the cellular to whole body levels, in particular exploring the utility of biomarkers in
diagnosis and monitoring disease process.
 To enhance interpretative, communicative, practical and data processing skills through

problem-based learning, presentations and laboratory experiences.
 To develop a constructive and critical appraisal of Clinical Biochemistry and the research
that underlies it, while encouraging interaction between staff and students and stimulating
independent study and research.
Credits - 4
Unit - I
Introduction to nutrition - Food as source of nutrients, functions of food, definition of nutrition,
nutrients & energy, adequate, optimum & good nutrition, malnutrition. Nutrition - Fitness,
Athletics & Sports. Food guide - Basic five food groups How to use food guide
Interrelationship between nutrition & health: - Visible symptoms of goods health. Use of food in
body - Digestion, Absorption, transport & utilization. Role of fibres in human nutrition. Effect
of cooking & heat processing on the nutritive value of foods. Processed supplementary foods.
Food sanitation in hygiene.
Unit – II
Introduction and maintenance of clinical biochemistry laboratory – hazards; units of
measurement; reference values – factors affecting reference values. Quality control in laboratory
– use of external and internal standards with WHO standards. Selection and evaluation of
methods. Automation in clinical laboratory; sources of biological variation. Collection and
preservation of samples. Sampling methods; Acid – base balance, Buffer systems. Role of lungs,
red blood cells, kidney in regulating the pH of body fluids. Metabolic and respiratory acidosis
26
07-08-2017
and alkalosis; mixed acidosis. Compensation mechanism. Tests used to evaluate acid-base status
of blood and their significance.
Unit – III
Functions of liver Metabolism of bilirubin – formation, transport, hepatic uptake and transport,
conjugation, excretion, bacterial degradation. Bile acid metabolism and formation and secretion
of bile; enterohepatic circulation; Liver function tests related to bilirubin, protein, carbohydrates,
lipid metabolism; Serum enzymes in liver disease. Jaundice – Classification, types, diagnosis and
differential diagnosis; Factors affecting enzyme levels in plasma or serum. Selection of enzyme
tests. Plasma enzymes in diagnosis and prognosis – aminotransferases, Creatine Kinase, LDH.
Unit - IV
Introduction: Chemistry, composition & functions of lymph, CSF, Ascitic fluid, and Synovial
fluid. Organ function tests: Kidney function tests, Pancreatic function tests, Gastric function
tests. Biochemistry of Diabetes mellitus, Fatty liver, and obesity. Diagnostic tests for HDL-
cholesterol, LDL-cholesterol and triglyceride disorders.
List of Practicals: (Nutrition and Clinical Biochemistry)
1. Estimation of blood glucose.
2. Estimation of blood urea.
3. Estimation of Creatinine in serum.
4. Estimation of uric acid in serum.
5. Estimation of serum total protein.
6. Estimation of Serum bilirubin.
7. Tests for abnormal constituents in urine.
8. Determination of urine ascorbic acid.
Outcomes:
 Evaluate nutrition information based on scientific reasoning.
 Provide nutrition education to individuals, groups, and communities throughout the

lifespan using a variety of communication strategies.
 Utilize technical skills and knowledge of health behavior when providing nutrition
recommendations to individuals across the lifespan.
 Identify strategies for food access, procurement, preparation, and safety for individuals,
families, and communities.
 Utilize knowledge from the physical and biological sciences as a basis for understanding
the role of food and nutrients in health and disease processes.
27
07-08-2017
 Exhibit knowledge of body chemistry levels under healthy or abnormal conditions.
 Accurately record and report results, indicating normal and abnormal values.
 Evaluate quality control results and note trends, shifts and invalid results.
 Explain the principles of the procedures and describe the clinical importance of
abnormalities.
Suggested Readings: (Nutrition and Clinical Biochemistry)

1. Textbook of Medical Biochemistry By MN Chatterjea and Rana Shinde, Jaypee Brothers.
2. Medical Biochemistry (Paperback) By John W. Baynes and Marek Dominiczak.
Publisher: Mosby.
3. Clinical Biochemistry: An Illustrated Colour Text (Paperback) 3rd Ed By Allan Gaw,
Michael Murphy, Robert Cowan, Denis O'Reilly, Michael Stewart and James Shepherd.
Publisher: Churchill Livingstone.
4. Review of Medical Physiology (Lange Basic Science) (Paperback) By William F.
Ganong. Publisher: McGraw-Hilll Medical
5. Harper's Biochemistry (Lange Medical Books) (Paperback) By Robert K. Murray, Daryl
K. Granner, Peter A. Mayes and Victor W. Rodwell. Publisher: Appelton and Lange.
28
07-08-2017
SEMESTER III
PAPER IV - ENDOCRINOLOGY, DEVELOPMENTAL BIOLOGY AND PHYSIOLOGY
Objectives:
 To study the structure and function of endocrine glands.

 To understand the mechanisms of hormonal action.
 To study the clinical disorders of hormones.
 To understand the cell to cell communication.
 To study the human physiology.
Credits - 4
Unit – I
Endocrinology
General Principles of Endocrinology; What are hormones, types of release and homeostasis
Mechanism of action of hormones:- Genomic and non-genomic; Peptide Hormones, Steroids,
catecholamines and prostaglandins.Chemistry, functions and synthesis of steroid, Polypeptide
hormones, Thyroid hormones.Hormones of pancreas and parathyroid.Clinical disorders of
hormones.Hormone receptors. Metabolism I – The Endocrine Pancreas, Pancreatic Anatomy,
Insulin and Glucagon. Metabolism II – Pancreatic Functions, Metabolism, Gluconeogenesis,
Diabetes, Feeding.
Unit – II
Endocrinology
The Hypothalamus-hypophyseal system I- Anatomy, Tropic Hormones. The Hypothalamus-
hypophyseal II-Tropic hormone regulation.The Hypothalamic-Pituitary System III.Tropic
hormone regulation; Vasopressin, and Oxytocin, melatonin. Gastrointestinal Hormones: Pepsin,
Gastrin, Secretin, and Cholecystokinin. Parathyroid hormone, Calcitonin, Adrenal Steroids,
Adrenal anatomy, Aldosterone, Adrenal Medulla, Calcium and Phosphate Homeostasis.
Unit – III
Developmental Biology
Introduction to Developmental biology. History and Basic concepts. Gametogenesis, Isogamy
and Anisogamy. Spermatogenesis vs. Oogenesis. Fertilization. Sperm and Egg Recognition.
Sperm and Egg Binding. Membrane and Pronuclear Fusion. Mechanisms of Preventing
Polyspermy. Fertilized-Egg Activation. Genes and Development. Early evidences for genes.
Differential gene expressions. Developmental Genetics. Mechanisms of differentiation-
induction, asymmetric division, morphogens. Self-organization-Cell adhesion, Extracellular
matrix. Fertilization in animals and Plants. Cell-Cell signalling. Polarity and the organizer.
29
07-08-2017
Unit – IV
Physiology
Units of Human system – Structure-function relationship of a cell and different tissues, structure,
distribution, characteristic features of epithelial, connective, muscular and nervous tissues.
Organization of the cell and its functions. Intercellular communications. Transport across cell
membrane. Membrane potentials. Mechanism of muscle contraction and its molecular basis,
types of contraction – isotonic and isometric contractions. Energetics of muscle contraction –
Rigor mortis. Types and properties of muscle fiber. Structure and types of smooth muscle.
Contraction of smooth muscle.
List of Practicals: (Endocrinology, Developmental Biology and Physiology)

1. Estimation of thyroxine from human blood
2. Determination of Acetylcholine esterase
3. Assay of enzyme activity
4. Isolation and estimation of serum cholesterol
5. Cleavage, Blastocyst, Gastrulation
6. Determination of bleeding time (BT) and clotting time (CT)
7. Determination of blood groups (A,B, and O system)
8. Determination of erythrocyte sedimentation rate (ESR) and packed cell volume (PCV)
Outcome:
 Will be able to understand the important role of endocrine gland system.
 Will be able to know how hormones are important and their abnormal effects.
 Will be able to understand the concepts of developmental biology such as male and
female gametogenesis, fertilization and the genes involved in development process of
embryo.
 Understand how the human system is developed, what are the basic units as well as how
cells, tissues and organs are developed.
Suggested Readings: (Endocrinology, Developmental Biology and Physiology)

1. Endocrinology. An Integrated Approach. Stephen Nussey and Saffron Whitehead. Oxford
Press, 2001.
2. Text book of Endocrinology and Diabetes 2edi. John AH.Wass, Paul M. Stewart,
Stephanie A. Amiel and Melanie C.Davies. Oxford Press, 2011.
3. Gilbert S. Developmental Biology. 10th Edition. Sinauer
4. JMW.Slack. Essential Developmental Biology. 3rd Edition, Wiley-Blackwell, 2012.
30
07-08-2017
5. Christiane Nusslein-Volhard. Coming to life: How genes Drive Development. Kales

press, 2006.
6. Lewis Wolpert. Developmental Biology; A very short introduction. Oxford university
press, UK. 2011.
7. Guyton (Arthur C), Text of Medical Physiology 11th Edition, 2008, Prism Publishers,
Bangalore.
8. Ganong (William F), Review of Medical Physiology, 23rd Edition, Lange.
9. Chaudhuri (Sujith K), 5th Edition Concise Medical Physiology New Central Books,
Calcutta.
th
10. Tortora (Gerald J), Principles of anatomy and physiology 11 Edition John Waley &
Sons, Ref. college publication.
31
07-08-2017
Semester Title of the Paper Credits Max. marks Min. marks

Theory
I. Recombinant DNA 4 100 35
technology
II. Proteomics and 4 100 35
Genomics
IV
Practicals
I. Recombinant DNA 2 50 18
technology
II. Proteomics and 2 50 18
Genomics
Project 8 200
Viva-voce 4 100
Total Credits: 24C – Theory – 08C; Practicals – 04C;
Project – 08C; Viva-voce – 04C
Total marks – 600 (200+50+50+200+100)
Seminar - 10 M
32
07-08-2017
SEMESTER IV
PAPER I – RECOMBINANT DNA TECHNOLOGY
Credits – 4
Objectives:
 To illustrate creative use of modern tools and techniques for manipulation and analysis of
genomic sequences.
 To expose students to application of recombinant DNA technology in biotechnological

research.
 To train students in strategizing research methodologies employing genetic engineering

techniques.
 To study the application of biotechnology in medicine.

 To study the application of biotechnology in veterinary.
Unit –I
General Introduction and Achievements of Biotechnology:
Genetic Engineering and r-DNA technology, Enzymes used in rDNA Technology (Restriction
Endonucleases, DNA Ligases, Topoisomerases, Methylases, Nucleases, Polymerases, Reverse
Transciptase and their Properties and Functions). Cloning Vectors (Plasmids, Phage, Cosmids,
Yeast, PBR322 and its derivatives), Viral Vectors (SV40 and Baculovirus) used in Gene Cloning
strategies. Cloning and Selection strategies and Screening analysis of Recombinants (Single
Colony Hybridization technique, Fluorescence, In situ Hybridization).
Unit–II
Introduction of Recombinant DNA molecules into Appropriate Hosts – Competent cells
preparation, Electroporation, Microinjection and Particle Bombardment method and Selection of
Transformants. Expression of Cloned Genes – Construction of Expression Vectors. Vectors
having Inducible lac, taq promoters. Expression of proteins with His tag and its significance in
simultaneous expression. DNA Finger Printing – RAPD, RFLP and AFLP Analysis.
Unit–III
Application of Biotechnology in Medicine: Production of Growth Hormone, Concepts of Tissue
engineering - Skin, Liver, Kidney and Heart. Principles and Species suitability for Aquaculture
(Indian major carps and Prawns). Genetic status of Culture stocks. Chromosome Manipulations -
Production of all Male and Sterile populations and Hypophysation in Fishes and Prawns. Gene
therapy: Adenosine-deaminase deficiency disease (ADA), Duchenne Muscular Disease (DMD),
Haemophilia, Phenylketonuria, Alkaptonuria and Thalassemia.
33
07-08-2017
Unit–Iv
Application of Biotechnology in Veterinary: In vitro Fertilization - Concepts of Superovulation,
Collection, Maintenance and Maturation of Oocytes, Fertilization of Oocytes, Maintenance and
Assessment of Embryos, Embryo transfer, Artificial Insemination, Preparation of Foster Mother,
Surgical and Non-surgical methods of Embryo transfer, Donor and Recipient aftercare. Cloning
concept of Nuclear transfer, Nuclear reprogramming and Creation of Dolly. Stem Cells Isolation
and Culture, Embryonic and Adult Stem Cells, Plasticity and Concept of Regenerative Medicine.
Transgenic Animals - Retroviral, Microinjection and Engineered Embryonic Stem Cell method
of Transgenesis. Application of Transgenic Animals – Biopharming. Disease Models and
Functional Knockouts.
List of Practicals: (Recombinant DNA Technology)
1. Problems related to Molecular Genetics.

2. Southern and Western blotting.
3. Electro – elution of DNA.
4. Restriction digestion of DNA.
5. Separation of RE –digested fragments by Gel Electrophoresis.
6. Restriction Mapping of a Plasmid.
7. Polymerase Chain Reaction.
8. Instrumentation in Animal Biotechnology Laboratory.
9. Staining and Viability testing of Animal cells.
10. Sterilization techniques (Physical and Chemical).
11. Animal Cell Culture and Characteristics.
12. Isolation of DNA from Blood Sample.
13. Transgenic Animals.
Outcomes:
 Technical know-how on versatile techniques in recombinant DNA technology.
 An understanding on application of genetic engineering techniques in basic and
applied experimental biology.
 Proficiency in designing and conducting experiments involving genetic manipulation.

 Explain the underlying mechanisms of gene cloning.
 describe recombinant gene expression systems.
Reference Books:
1. L.M.Narayanan, A.Mani, A.M.Selvaraj and N.Arumugam – Molecular Biology &

Genetic Engineering, Saras Publications.
2. D.Balasubramanian and CFA Bryce – Concepts in Biotechnology, University Press.
34
07-08-2017
3. Agarwal – Text book of Biochemistry, Goel Publishers, Meerut.

4. Gerald and Kalp – Cell and Molecular Biology (Concepts & Experiments), John
Wiley & Sons, USA.
5. Martin Clynes - Animal Cell culture Techniques, Springer.
35
07-08-2017
SEMESTER IV
PAPER II – PROTEOMICS AND GENOMICS
Objectives:
 Will provide both theoretical and practical training in the use of quantitative proteomics
approaches.
 Participants will learn the principles of current methodologies including SILAC and
TMT-based as well as targeted proteomics.
 Will be trained in the use of bioinformatic tools for data analysis.
 Will explain some of the current genomics technologies and illustrate how these can be
used to study gene function.
Credits - 4
Unit – I
Genome – Definition, Difference between gene and genome. Genome sequences, Transcriptome
and Transcriptomics. What are micro arrays, Differences between macro arrays and micro
arrays,Gene/biochips, Gene expressions by microarray technology, Applications of Microarray.
Unit – II
Metabolomes – Metabolomics, Analysis of metabolites using different analytical techniques, Use
of metabolomics in microbial, plant and animal studies. Biological mass spectrometry (MS),
Tandem mass spectrometry (MS-MS).
Unit – III
Protein, Proteomics, Separation of proteins by 2- Dimensional gel electrophoresis. Advantages of
proteomics over genomics. Methods of protein in-gel digestion, peptide mass finding using
biological mass spectrophotometer. MALDI-TOF, MALDI-TOF/TOF, Q-TOF (Quadrapole time
of flight) for protein identification and annotation. Protein annotation based on peptide
sequencing.
Unit – IV
CRISPER Cas-9 technique in genome editing, siRNA, miRNA, shRNA, gene silencing.
Advantages of CRISPER Cas-9 technology for generating animals and plants of interest with
desired charcters. Use of CRISPER Cas-9 for human health care.
36
07-08-2017
List of Practicals: (Proteomics and Genomics)

1. Isolation of RNA either from plants or animal tissues.
2. Conversion of RNA into cDNA using cDNA kit.
3. Estimation of RNA using UV-VIS spectrophotometric method
4. Expression of any gene using quantitative real-time PCR method.
5. Protein-protein interaction studies using the tools of bioinformatics.
6. In silico proteome analysis using mass spectrometry
Outcomes:
 Design quantitative proteomic experiments, including selection of the most appropriate
hardware and software.
 Analyse quantitative proteomic data by various software tools.
 Evaluate the quality of proteomic data sets.
 Describe recent advances in genomics, transcriptomics, metabolomics and proteomics.
 Obtain and analyse information and data relating to specific genes using a number of
general and plant-specific databases, bioinformatics principles and tools.
 Perform a range of practical techniques including DNA sequencing, PCR and proteomics.
 Design a set of experiments to address a particular biological question.
Suggested Readings: (Proteomics and Genomics)

1. Principles of Gene manipulation and Genomics – By S.B.Primrose and Trawman,
Published by Singer and Berg
2. Genomics Hand book - By Rosanna Mann
3. Genetics and Genomics – By Pearson
4. Introduction to Genomics – By Arther M. Lesk
5. Discovering Genomics, Proteomics and Bioinformatics – By Malcolm Campbell
6. Introduction to Proteomics – By Josip Lovric
7. Proteomics : Concepts, Techniques and Applications – By Aubhishek Zaman
37
07-08-2017
38
07-08-2017
SEMESTER IV
The candidate should submit a project report by the end of final year course on a topic relevant
Biochemistry, based on the laboratory experiments/case studies/field studies carried out in
Biochemistry/related industry and should give a seminar on the project work and should defend
in viva-voce.
PROJECT 8C
Project Dissertation & VIVA – VOCE 4C
39

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1 M.

Semester Title of the Paper Credits Max. Min.

Total Credits: 24C – Theory – 16C; Practicals – 08C

Total marks – 600 (400+50+50+50+50)

Marks allocation for theory examinations:

Max. Marks 100 – Theory main exam - 70M

Internal Assessment - 20M

Unit –II: Nomenclature of chromosome; C-value paradox; Organization of Eukaryotic

1. Preparation of Cytological slides for Mitosis using Root tips.

Suggested Readings: (Cell Biology)

Objectives: On completion of this course the student will be able to

Understand the taxonomy and of classification of microbes.

List of Practicals: (Basic Microbiology)

Suggested Readings: (Basic Microbiology)

4. A. Mani, A. M. Selvaraj, L.M. Narayanan and N. Arumugam – Microbiology, Saras

 To learn about fundamentals of Chemical foundations of Biology.

Suggested Readings: (Biomolecules – Structure and Function)

 To study the structure and function of immune system.

List of Practicals: (Immunology)

Suggested Readings: (Immunology)

Semester Title of the Paper Credits Max. Min.

Total Credits: 24C – Theory – 16C; Practicals – 08C

Total marks – 600 (400+50+50+50+50)

Marks allocation for theory examinations:

Max. Marks 100 – Theory main exam - 70M

Internal Assessment - 20M

o To study the Mendel principles of Genetics and Genetic Recombination.

Emphasis on Darwinism and Lamarckism.Neo-Darwinism.An account on destabilizing forces:

List of Practicals: (Genetics and Evolution)

 The students will be able to differentiate different models in Homologous recombination.

Suggested Readings: (Genetics and Evolution)

 To learn the mechanisms of action of enzymes and inhibitors.

 To introduce students to various theoretical and practical aspects of enzymology.

 The students will be able to differentiate different models in Homologous recombination.

Suggested Readings: (Enzymology)

List of Practicals: (Tools and Techniques in Biology)

Outcomes of the course:

Suggested Readings: (Tools and Techniques in Biology)

 Restate the two Laws of Thermodynamics.

List of Practicals: (Bioenergetics and Intermediary Metabolism)

 Learn importance of thermodynamics in living systems.

 Explore the consequences of energy, thermodynamics laws and significant of chemical

Suggested Readings: (Bioenergetics and Intermediary Metabolism I&II)

Semester Title of the Paper Credits Max. Min.

Total Credits: 24C – Theory – 16C; Practicals – 08C

Total marks – 600 (400+50+50+50+50)

Marks allocation for theory examinations:

Max. Marks 100 – Theory main exam - 70M

Internal Assessment - 20M

On completion of this paper/module, you will be able to -

List of Practicals: (Molecular Biology)

Suggested Readings: (Molecular Biology)

 To make proper use of raw data.

 To study the development of computational methods to utilize expression data to reverse

 To study of population genetics and its connection to human disease.

Overview of primary, secondary structural elements. Protein secondary prediction, Introduction

List of Practicals: (Biometry, Biostatistics and Bioinformatics)

 To enhance knowledge of nutrition and metabolism and the application of such

 To provide an organization which encompasses the needs of professionals from all

 To develop a detailed awareness of specific clinical biochemistry topics studying from

 To enhance interpretative, communicative, practical and data processing skills through

 Evaluate nutrition information based on scientific reasoning.

 Provide nutrition education to individuals, groups, and communities throughout the