AC 10/02/12

Item No. 4.26

UNIVERSITY OF MUMBAI

Program: M.Sc.
Course : Biophysics
Syllabus for the Semester I & II

(Credit Based Semester and Grading System with

effect from the academic year 2012–2013)
Preamble

The subject of Biophysics is one of the important interdisciplinary areas in teaching, training and learning
which is considered to be important in terms of human resource development and National development.

Biophysics is the physics of life phenomenon studied at all level, from molecules and cell to the biosphere as
whole. It may be defined: Biophysics is that branch of knowledge that applies the principles of physics and
chemistry and the methods of mathematical analysis and computer modeling to understand how biological
systems work.

The main emphasis of biophysics is on the quantitative analysis of the physical and chemical aspects of the
functions of biological molecules, organisms and entities. The techniques and methodologies that biophysics
relies on are closer to Physics and Chemistry, but areas of application are in the biological, medical and
related sciences

Biophysicists use a variety of techniques such as UV visible spectroscopy, Gel electrophoresis, X-ray
crystallography, microcalorimetry, Atomic Force Microscope, FTIR, Raman, SPR, NMR, fluorescence
spectroscopy, Fluorescence Microscopy, Viscometry, G M Counter etc are used to study problem in
exciting areas in biophysics ranging from structure aided drug design to cell signalling and transcriptional
silencing etc.

Biophysicist works in Universities, R & D industry, Medical Centres/Colleges, Research Institutes,

Government Organisation etc.

The two year programme of M.Sc. (Biophysics) is prescribed according to the credit system of University of
Mumbai from the academic year 2012-13. The course has been divided in to four semesters. The programm
has total 16 theory papers, and four in each semester.

The programme is designed to provide students a broad based training in Biophysics with strong background
of basic concepts as well as exposing them to the advanced fields. In addition to theoretical knowledge,
significant emphasis has been given to provide hands on experience to the students in the frontier areas of
Biophysics. A multidisciplinary approach has been employed to provide best leverage to students to enable
them move into advanced and frontier areas of biological research in the future. Hence, one paper is also
introduced on soft skill as per the guideline given by University of Mumbai. This paper focusses on
perception, comprehensive, presentation skills etc. This will enable to add new dimension in frontier
research skills in students.

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 Revised syllabus of M.Sc. Biophysics
Semester I & II
(Based on Credit and grading system)
Semester I
Paper Paper nomenclature Lectures Credit Practical Hrs Credit Total
code Paper No & Credit
Code
PSBP101 General Physico-chemical 60 04 Paper I 60 02 06
Principles (PSBPP 101)

PSBP102 Biomathematics & 60 04 Paper II 60 02 06

Biostatistics (PSBPP 102)

PSBP103 Cell Biophysics 60 04 Paper III 60 02 06

(PSBPP 103)

PSBP104 Methods in Biophysics 60 04 Paper IV 60 02 06

(PSBPP 104)

Total 24
Semester II
PSBP 201 Molecular Biophysics 60 04 Paper V 60 02 06
(PSBPP 201)

PSBP202 Biochemistry 60 04 Paper VI 60 02 06

(PSBPP 202)

PSBP203 Molecular Biology & 60 04 Paper VII 60 02 06

Protein Engineering (PSBPP 203)

PSBP204 Membrane Biophysics 60 04 Paper VIII 60 02 06

(PSBPP 204)

Total 24
Grand Total (Sem I & II) 48

Total credits for M.Sc. Part I =(Sem I‐ 24 and sem II‐24) =48

Evaluation: The students will be evaluated internally and externally. The internal evaluation is done by
concern teacher and external evaluation done by the committee appointed by the University norms. Standard
passing and scale as per the university norms.

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 M.Sc. BioPhysics Syllabus
Semester I & II
Credit Based and Grading System
To be implemented from the Academic year 2012-2013
SEM: I
Paper I: General Physico-chemical Principles: PSBP101
Paper II: Biomathematics & Biostastics: PSBP102
Paper II: Cell Biophysics: PSBP103
Paper III: Methods in Biophysics: PSBP104
SEM: II
Paper IV: Molecular Biophysics: PSBP201
Paper V: Biochemistry: PSBP202
Paper VI: Molecular Biology & Protein Engineering: PSBP203
Paper VIII: Membrane Biophysics: PSBP204

SEMESTER I

General Physico-chemical Principles: PSBP101

Course Code UNIT TOPIC HEADINGS Credits L / Week

I Laws of Physics and Chemistry
II Energies Forces & Bonds
III Principles of Kinetics of Molecules
PSBP101 4
IV Proton Transfer equilibria
Electron Transport & Oxidative
V
phosphorylation
Biomathematics & Biostatistics PSBP 102

I Introduction to Biomathamatics
II General principals
PSBP102 4
III Introduction to statistics
IV Hypothesis and Tests
Cell Biophysics: PSBP103

I General organisation of cell

II Cell differentiation
PSBP103 4
III Cell growth & Division
IV Cell cell communication
Methods in Biophysics: PSBP 104

I Spectroscopy
PSBP104 4
II Microscopy
4
 III Separation Techniques

General Biophysics
1. PH Meter: Standardization of pH meter,
Preparation of Buffers,
2. pH titration curve of acid-base
3. Determination values of Iso-electric
point: Amino acids, proteins, phosphoric
acids.
4. Viscosity: Determination of viscosity of
PSBPP101 biofluids and chemicals 2
5. Colorimeter: Verification of Beer’s-
Lambert law, determiantion of absorption
maxima of color compounds,
determination of molecular extinction
coefficient.
6. Estimation of percent purities of dyes and
inorganic compound

Biomathematics & Stat

1. Calculation of measures of dispersion: a)
Mean deviation b) std deviation and
coefficient variation c) Quartile deviation
2. Test of significance: a) Chi-square test b)
PSBPP102 t-test 2
3. To evaluate standard error and
interpretation of results of accuracy and
precision

Cell Biophysics
1. Microscopy: Familiarizes with
bright field , phase contrast,
fluorescent, polarization microscopes.
2. Classification of gram –ve & +ve
ogananisms
3. Observe cell growth/ survival by
colony forming assay
PSBPP103 4. Estimation of cell viability by dye 2
exclusion and colony techniques.
5. Observe cell death by physical and
chemical agents
6. Observe cell division and determine
mitotic index ( Demonstration)
7. Determination of cellular
carbohydrates by Acid shifts (PAS)
reaction.

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 8. Blood analysis: Total WBC count,
PCV, MCV etc
9. Differential Counts,
10. Total RBC count,
11. Blood grouping and coagulation.
12. Hemoglobin estimation.

Methods in Biophysics (Practical)

1. Fractionation of proteins using: PAGE,
PAPER electrophoresis
2. TLC: Amino acids/ sugars/ fruit juice/oil
3. Column chromatography for protein
PSBPP104 /pigment 2
4. To study of conformational changes in
biomolecules using Ostwald viscometer
5. Refractoemetry: study of
sugars/proteins/amino acids

SEMESTER II

Molecular Biophysics: PSBP201

Principles of protein structure &

I
confirmation
II Proteins structure and stability
PSBP201 4
III Structure of Nucleic Acids
Molecular distribution & statistical
IV
thermodynamics

Biochemistry: PSBP202

Course Code UNIT TOPIC HEADINGS Credits L / Week

I Hormones & its Actions
II DNA structure, Replication & Repairs
PSBP202 III RNA synthesis & Translation 4

Regulation of gene expression in

IV
prokaryotes
V Ligand receptors & Interactions

6
Molecular Biology & Protein engineering: PSBP203

Course Code UNIT TOPIC HEADINGS Credits L / Week

Preparation and analysis of DNA,
I Enzymatic manipulation of DNA &
RNA
Construction of Recombinant DNA
II
libraries & In vitro Mutagenesis
PSBP203 Introduction of DNA into mammalian 4
III cell & system for study of cloned
Genes
Micro sequencing methods for
IV proteins & Engineering proteins for
purification
Chemical approach to protein
V engineering & Protein engineering for
thermostability

Membrane Biophysics: PSBP 204

I Membrane structure & Models

II Physical properties of membrane
III Membrane transport 4
PSBP204
IV Molecular dynamics of Membrane
Membrane potentials & Lipid
V
membrane technology

Molecular Biophysics (Practical)

1. Study of thermal denaturation of DNA
and protein
2. Mutarotation of glucose and amino
acids
3. Study of DNA-Protein interaction
using fluorometry
4. Study of fluorescence sensitivity and
PSBPP201 quenching 2
5. Absorption spectra of Hb, DNA,RNA
etc
6. Study of interaction of acridene orange
with DNA
7. Identification of C-terminal and N-
terminal amino acid

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 Biochemistry (Practical)
1. Enzyme Assays (LKH, beta
galacotsidase, acid phophotase,
arginase, Succinic De –hydrogenase) :
Time , Temp, Protein concentration,
cofactors. LKH: Km & Vmax.
PSBPP202 2. Estimation of Protein by 2
Lowery/Biuret/ Bradford methods
3. Isolation of casein protein from milk,
Hb from RBC
4. Assessment of antioxidants /Lipid
peroxidation from given samples.

Molecular Biology & Protein Engineering

(Practical)

1. Isolation of DNA (Nuclear &

Mitochondrial)
2. Detection of DNA modifications.
3. Restriction endonuclease digestion and
separation of fragments by gel
PSBPP203 electrophoresis. 2
4. Determination of base composition of
Nucleic acids
5. Gel filtrations chromatography
6. To find out capacity & nature of the given
ion exchange resin.
7. DEAE cellulose chromatography of DNA
8. PCR ( Demonstration)

Membrane Biophysics (Practical)

1. Preparation of liposome’s / artificial
membrane: Lipid mixture/ BSA /
Ovalbumin (Demo)
2. Fluorescence anisotropy and polarization
measurement
3. Protein tryptophan fluorescent
measurement.
PSBPP204 4. Study of membrane fluidity. 2
5. Effect of hypertonic/ hypotonic/isotonic
on RBC membrane.
6. Purification of substances by dialysis
7. Study of volume regulation of erythrocyte
and osmotic fragility.
8. Ionophore effect on erythrocyte.
9. Osmolarity: Determination of osmotic
pressure of salts.

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 10. Verification of fick’s law of diffusion
11. Study of phase transition of membrane
phospholipids
12. To study of membrane potential using
fluorescence spectroscopy

Semester I Detail Syllabus

Course Code Title Credits

PSBP 101 General Physico-chemical Principles 4
Total lectures:60
Unit I: Structure & Bonding: Quantum mechanics: Pauli Exclusion Principle,
Ionization energy, electron affinity and chemical binding, Electronegativity and strong bonds,
secondary bonds. The electronics structure of atoms, Molecular orbital and Covalent bonds.
Molecular interaction: strong and weak interactions. Stereochemistry and Chirality, 20L

Unit II: Thermodynamics: Basics of Thermodynamics: Laws of thermodynamics and

living organisms, Entropy, Enthalpy, Efficiency and free energy of system, Concept o
energy in biological system, living body and thermodynamics, Carnot cycle, Chemical
potential. (20 L)

Unit III: Kinetics of Molecules & Reactions: 0th, 1st,2nd & 3rd order reactions, Diffusion,
Osmosis, Osmotic pressure, osmoregulation, surface tension, dialysis, adsorption, viscosity,
thermal conduction, collides, sedimentation. (10L)
Unit : IV Acid-Base equilibrium: Bronsted lowry theory, protonationa and deprotonation,
buffers, amphiprotic system, protolysis of water, hydrogen ion concentration, pH, acid base
balance, Henderson and Hasselbalch equation. (10L)

References:
1. Physical Chemistry for Life Sciences,Peter Atkins and Julio de Paula, 2006, Oxford
Press
2. Introduction to Biophysics by Cortell
3. Molecular and Cellular Biophysics, Meyer B Jackson (2006), Cambridge)
4. Tex Book of Biophysics , R N Roy, New Central Agency (P) Ltd, Culcutta
5. Physical Chemistry for the Biosciences, Raymond Chang,(2004), University book
Science Biological Thermodyanamics, Donald, T Hayine, (2007), Cambridge

Course Code Title Credits

PSBP102 Biomathematics & Biostatistics 4
Total lectures: 60
Unit I:Biomathematics
Limits of functions, derivatives of functions. Probability Calculation, Differential and
integral calculus, Derivative and its physical significance, basic rules for
differentiation (Without derivation) Maximum and Minimum their application in

9
chemistry, Geometric meaning of integration, application in biology and chemistry.
(15L)

Unit II: Biostatistics I

1. Introduction, scope, application and use of statistics, collection and
classification of data, census and sampling, graphs and diagrams, arithmetic
mean, median standard deviation.
2. Correlation and regression for ungrouped data, scatter diagram, calculation
and interpretation of correlation coefficient, linear regression coefficients and
equation of the Lines of regression, nonlinear relationship transformable to
liner form (Y=Abx, Yaxb)
3. Probability, definition, addition and multiplicative laws (without proof).
Random variable and its distribution, binominal probability distribution,
examples and condition s means and Variances, continuous variable, normal
distribution, use of normal probability table for finding probabilities. (15L)
Unit III: Biostatistics’ II
1. Population parameter and sample statistics, sampling techniques, simple
random sampling stratified random sampling, systematic sampling standard
error of mean.
2. Estimation, Point & interval, confidence interval for proportion.
3. Hypothesis attesting, Type I and Type II errors levels of significance, one-
tailed and two tailed test, application to single proportion, equality of the
population means and two population proportions.
4. Chi-square test for independent attributes in r x c table, special case of 2 x 2
tables.
5. Students test for significance of correlation coefficient y fore p=0 (small
sample test (15L)
Unit IV: Biostatistics III
1. Fishers z transformation coefficient for getting yp-0 in large samples test of
significance For y (p=0)
2. Design of experiment: Principle and concepts of completely randomized
design, randomized block design and Latin square design,
3. variance ratio F-test-Analysis of variance in one-way classification .
4. Non-parametric test: Distribution-free method, sign test for method pairs,
Wilcoxon test for unpaired data Run test. (15L)

References:
1. Biostastistics:A foundation for analysis in the Health Sciences, 7th Ed.(1998) Wayne
D, Wiley
2. DNA Microarrays, David Bowtell & J Sambrook (2002), CSHL Press
3. Principles of Statistics, 2nd Ed. M Pagano & K Gauvreau (2007), Thomson Publ

10
Course Code Title Credits
PSBP 103 Cell Biophysics 4
Total lectures:60
Unit I: General organization of cells: Discovery of Cell, Shape & Size of cell, General
organization of prokaryotic and eukaryotic organisms’ basic concepts and their detailed
structure functions, Prokaryotic cell Wall, Eukaryotic cell wall, functions of cell wall,
Physical & Biological properties of cytoplasm, (15L)

Unit II: Cell Differentiation: Cellular differentiation; localization of cytoplasm

determinants in egg. Nucleocytoplasmic interaction and cell function, Development
of extra cellular matrix, mechanism of alpha adrenergic and related response,
modulation of extra cellular matrix by tumor cell- Fibroblast interactions, growth
factors in cultured cell-early cytoplasm singles and Cytoskeleton responses. (15L)

Unit III :Cell growth and Division: Kinetics of cell growth, Role of protein kinase
in cell growth, cell cycle, cell cycle events: G S G2, Cell division, cytokines, control of
cell cycle, Role of protein kinase c in cell growth, dividing and non‐dividing cell,
synchronization of cell growth, cell transformation, malignant tumor growth,
Apoptosis. (15L)

Unit IV : Cell-Cell Communication: Strategies of chemical signaling: Endocrine,

paracrine and synaptic. Signaling mediated by intracellular receptors: Mechanisms of
transduction by cell surface receptor protein, role of calmodulin, Ca and cyclic
nucleotides, phosphoinisitol cycle, sodium proton exchanger, molecular events
involved in during sperm-egg interaction, implications and the mechanisms of sperm-
zone interaction, Role of soluble factors produced by follicle somatic cell on gamete
interactions. Factors influencing sperm egg recognition and binding.
(15L)
References:
1. Molecular Biology of the Cell, Bruce Albert, Alexander Jhonson et al (2002),
Taylor & Francis Group.
2. The Cell Molecular Approach, G Cooper & R Hausman (2007) ASM Press
3. Molecular Biology , D Roberties, 8th Ed. SAE
4. Biochemistry by Strayer
5. Introduction to Biological Membrane, D Chapman
6. Molecular Cell Biology, Lodish
7. Molecular and Cellular Biophysics, Meyer B Jackson (2006), Cambridge)

11
Course Code Title Credits
Methods in Biophysics
PSBP104 4
Total Lectures:60
Unit I: Spectroscopy: Principle, instruments and application of spectroscopic instruments:
UV Visible: absorption of light, radiation sources, sample holders, monochroamtors,
radiation detectors, single and double beam instruments, Colorimeter. IR spectroscopy:
Rotational and vibration spectra, Instrumental features, applications. Raman: Raman effect,
stokes and anti-stokes lines, advantages, applications. CD ORD principles and applications.
Fluorescence: Fluoresces and phosphorescence phenomenon, quenching, energy transfer, and
applications. Atomic absorption spectroscopy: Principle and instrumentations. (15L)

Unit II: Microscopy: Principle, instrumentation and application of Microscopy, image

formation, magnification, resolving power. Different types of Micrscopy: Dark field ,Phase
contrast, polarization microscopy, Fluorescence, Electron microscopy: Electron guns,
Electron lens, (15L)

Unit III:Separation techniques I: Electrokinetics methods: electrophoresis,

electrophoretic mobility (EPM), factors affecting EPM, Paper, PAGE, Capillary, Iso-Electric
focusing, applications in biology and medicine. (15L)

Unit IV: Separation technique II: HPLC: mobile phase systems, modes of operations,
application, Hydrodynamics method: fundamental principles, Centrifugation,
Ultracentrifugation and their applications in molecular weight, size determination. Viscosity
and its application (15L)
References
1. Methods in Molecular Biophysics, Igor N S, N Zaccai & J Zaccai, (2007)
Cambridge
2. Principle of Biochemistry, D Voet, J Voet and CW Pratt, 3rd Ed,
3. DNA Clonning, Grover Vol. I, II, III
4. Advanced Methods in Protein Microsequencing, Witmann
5. Essential Biophysics, Narayanan, New Age Publ
6. Handbook of Molecular Biophysics (Methods & Application), 2009, HG Bohr,
Wiley

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 Semester II Detail Syllabus
Course Code Title Credits
Molecular Biophysics
PSBP 201 4
Total lectures:60
Unit I: Principles of proteins structure and confirmations: Basics problems of protein
structure, Polypeptide chain geometrics, estimates of potential energy, results of potential
energy calculations, hydrogen bonding, hydrobhobic interactions and water as universal
solvent in biological systems, Disruption of hydrophobic interactions by urea, ionic
interactions, hydrophobic versus ionic interactions, Disulfide bond, Ways of pairing N-half
cystine, formation of specific disulfide link, prediction of protein structure. (15L)

Unit II: Protein structure & stability: Two state model of protein stability, chemical
denaturation and stabilization, surface denaturation.

Principles of ionization equilibrium ionization of side chain, equilibria in proteins. Predicting

properties from amino acid composition, Usual amino acids. Primary structure sequencing of
polypeptide, hemoglobin, homologies in proteins, Secondary structure alpha and beta
confirmation, collagen structure, stability of alpha helix, Ramchandran plot, Tertiary
structure, structure of myoglobin and hemoglobin, Quaternary structure, symmetry
consideration, Analysis of subunits and chain arrangement of subunits, stability of globular
quaternary structure. Protein folding rules, pathways and kintetics. (15L)

Unit III: Structure of Nucleic Acids: Ionization equilibria of nuclosideand nucleotides:

compositions of nucleic acid, Chargaff’s rule in DNA, RNA base compositions, Primary
structure, Covalent chain structure, secondary structure inferences from RNA sequence
comparisons, sequence information and analysis of structure function. Structure DNA &
RNA (15)L

Unit IV: Molecular distribution and statistical thermodynamics: Binding small

molecule by polymer, identical and independent site model, nearest interaction and statistical
weight, cooperative binding, anticoperative binding and excluded site binding. The random
walk, Helix coil transition in protein. (15)

References:
1. Biophysical Chemistry, The Behaviour of biological macromolecules, Vol I,II, III,
Cantor and Schimmel, (2008), W H Freeman & Co
2. Applied Biophysics, A Molecualr Approach for Physical Scientist, Tom A Weigh,
(2007), Wiley
3. Introduction to Protein Sciences, Arthur M Lesk (2004), Oxford Press
4. Molecular and Cellular Biophysics, Meyer B Jackson (2006), Cambridge)
5. Chemical Biophysics, Daniel A Beard and Hong Q (2008), Cambridge Univ Press
6. Proteins Structure & Function, David Whitford (2005), Wiley
7. Introduction to Protein Structure, Carl Brenden & Jhon Tooze (1999), Garland Publ,
NY
8. Essentials of Biophysics, P Narayanan (2005), New Age Publ.
9. Physical Chemistry for Biomedical Sciences, S R Logan, (1998), Taylor & Francis.
10. Handbook of Molecular Biophysics (Methods & Application), 2009, HG Bohr,
Wiley
11. Principal of Protein Structure, GE Schulz, RH Schirmer (2004), Springer

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Course Code Title Credits
PSBP 202 Biochemistry 4
Total Lectures: 60
Unit I: Hormones and its action: Adrenocortical hormones, Thyroid hormones,
Insulin, glucagan. Action of cAMP/cGMP, G protein and G protein family receptor, G
protein cascades, c-AMP and protein kinase, protein phosporylation, Inositol triphosphate
and DAG signals. (15L)
Unit II: Replication and Repair: A B & Z DNA structure, major & minor groves in DNA,
Protein DNA interactions, supercoiling of DNA, Topoisomerase I and relaxed DNA, DNA
gyrase, eukaryotic gene.
Replication in vivo, semi-conservative mechanism of replication. Direction of replication.
Discovery of DNA polymerase I and its function. DNA synthesis in vitro, other DNA
polymerase, role of various proteins/enzymes in DNA synthesis. Model of DNA synthesis,
molecular basis of mutations, DNA repair mechanism, reverse transcription. (15L)

Unit III: Transcription & Translation: RNA polymerase and its action, promoter sites of
DNA template, sigma factor, elongation and termination of RNA chain, processing of
precursors-RNA,sn-RNA and tRNA, mRNA. RNA polymerase I and transcription of mRNA
in eukaryotic cells. Transcription factors in eukaryotes. Ribozyme and self splicing, genetic
code-discovery and silent features.
Recent advances, amino acid activation, fidelity of aminoacyl, tRNA synthesis, tyrosyl AMP
complex, tRNA structure and function. Ribosomal RNA structure, Architecture of EM and
neutron diffraction. Initiation of protein synthesis, translocation and peptide bond formation,
termination and stop codon, protein synthesis in eukaryotes. (15L)
Unit IV :Regulation of Gene expression in prokaryotes & Eukaryotes: Operator-
operon concept, Negative and positive control of transcription with example of lac operon
and Arbinose operon. Control of transcription, control of regulatory protein, transcription
termination, repressor, cro protein.
Eukaryotic RNA, role of histone, nuclosome, bidirectional replication, repetitive DNA,
transcriptiona; factor IIIA.
Ligand receptors interaction: Kinetics model based on steady state assumptions, allosteric
interactions and co-operative behavior regulation and control system in biology. (15L)

Reference:
Molecular cloning by Maniatis Vol. I, II, III
DNA cloning by Glover vol. I, II, III
Genome analysis a practical approach by devis.
Protein engineering practical approach by Reas.
Advanced method in protein micro sequence by Witmannn.
Principles of Biochemistry, Leninger (2008(, Freeman Publ

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Course Code Title Credits
Molecular Biology & Protein Engineering
PSBP203 4
Total Lectures: 60
Unit I: Preparation, analysis of DNA & Enzymatic Manipulation of DNA & RNA
: Genomic DNA from mammalian tissue plant tissue and bacteria resolution recovery
of large and small fragments of DNAS using various Electromagnetic techniques
chemical synthesis of oligonuleotides genes and their uses analysis of DNA’S
sequences by blotting and hybridization.
Restriction endonuclease and mapping Enzymes for modification and radioactive
labeling of nucleic acids, construction of hybrid DNA molecules. Polymerase chain
reaction. Preparation and analysis of RNA (15L).
Unit II: Construction of Recombinant DNA libraries: Genomic and c-DNA
libraries preparation of inserting DNA from genomic DNA and RNA production of
library and amplification. Screening of Recombinant DNA Libraries: Screening by
DNA hybridization Immunological assay and protein activity.
In vitro Mutagensis: Mutagenesiss with degenerate oligonuleotides region specific
Mutagenesis linker scanning Mutagenesis.
Introduction of DNA into Mammalian cell and System for study of cloned Genes:
Transformation of DNA using calcium Phosphate DEAE Dextrin and Elecroporation
and its optimization and uses. Bacterial Yeast expression vectors gene transfer Into
cultured cells. Development and use of transgenic animals. Manipulation and gene
Expression in prokaryotes, Heterogeneous protein production in eukaryotic cells
(15L)
Unit III:Micro sequencing Methods for proteins; Engineering proteins for
purification: Modern advancement such as Tar Sequencing Strategies. DABITC/
PITC methods. Solid phase mirosaequencing; Fast atom Bombardment (FAB) mass
spectra in protein sequencing.
Choice of purification tag, Enzyme purification Tags. Affinity purification tag, ion
exchange, hydrophane IC, covalent and chelae
Purification tags; PEG enzyme and PEG enzyme conjugates.(15L)
Unit IV: Chemical Approach to protein Engineering; protein engineering for
thermo stability: Functional group modification chimerical Protein, protein
engineering of Ab, combing sites, Directed Mutagenesis and protein Engineering.
Directed Mutagenesis procedure adding disulfide bonds changing asparaging to other
amino acid, reducing number of free sulphydryl residues increasing /modifying
Enzyme activity/specificity. Chemeric antibody replacement of FC domains,
catalytic Antibodies (enzymes) idiotype vaccines. Hybridoma technology.
stability estimates from denaturation curve , Engineering physical and biology
properties of protein by chemical modification, Antibody and site Mutagenesis,
supercritical fluid in protein extraction (15L)
Reference:
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 1. Molecular Clonning,Sambrook and Russell Vol 3, Cold Sprong Harbour lab press
2. Molecular and Cell biology, Lodish et al, (2004) Freeman
3. Electrophoresis in Practice, Reiner Westermeirer, (2005) Wiley
4. Methods in Molecular Biophysics Igor N S et al (2007), Wiley
5. Molecular cloning by Maniatis Vol. I, II, III
6. DNA cloning by Glover vol. I, II, III
7. Genome analysis a practical approach by devis.
8. Protein engineering practical approach by Reas.
9. Advanced method in protein micro sequence by Witmannn.
10. Principles of Biochemistry, Leninger (2008(, Freeman Publ

Course Code Title Credits

PSBP204 Membrane Biophysics 4
Total lecture: 60
Unit I:: Membrane structure and Models: Membrane architecture, Lipid vesicles
and planar Bilayer membrane, Membrane permeability, Membrane Channels,
transmembrane helices, hydropath Plot, Membrane Asymmetry, Membrane fluidity,
Functional reconstitution of membranes. Models of membrane fusion: bilayer fusion,
viral fusion, cellular fusion, SNAREs, cell-cell fusion, fusion in mitochondria, Lipid
bilayer and early models, Fluids mosaic model, Evidence from model system and
biomembranes. (15L)

Unit II: Physical Properties of membrane: Elastic properties, Elastic constants,

Charge-induced microstructures and domain. Hysteresis of domain formation. Lateral
phase separation. Critical concentrations fluctuation, selective lipid protein
interactions, Membrane melting. (15L)
Unit III: Membrane transport: Transport system with non-electrolytes and
electrolytes. Transport with chemical reaction system: Primary and secondary active
transport. Transports of molecules by simple and facilitated diffusion Transport by
flux coupling. Transport by phosphotransferase system, Transport by vesicle
formation
Electron Transport & Oxidative phosphorylation: Reduction potentials and free
energy changes in redox reaction, organization of electron transport chain,
chemiosmotic coupling, proton gradient drive and synthesis of ATP, P/O ratio for
oxidative phosphorylation, Cytosolic NADH electron feeding into electron transfer
(15L)
Unit IV: Membrane potentials & Lipid Membrane Technology: Cell surface
charge, Resting membrane potential, Action potential, properties of action potential,
Nernst equation, Hodgkin-Huxely equation, Membrane impedance and capacitance,
Transmembrane potential, Zeta, stern and total electrochemical potential,
Historical perspective of lipid model systems lipid monolayer. Liposomes: small and
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large unilamellar and multilamellar vesicles, planner lipid bilayer, Application of
liposomes in biology and medicine. (15L)
References:
1. Molecular & Cellular Biology, D Roberties,
2. Biophysical Aspects of Transmembrane signaling, Sandor D (2005), Springer
3. Biophysics, Vasant Pattabhi, Gautam (2002), Narosa
4. Biomembrane structure and Function, Chapman D.
5. Introduction to Biological Membrane, Jain R K
6. Biophysics, Hopp, Lohman, Mark and Ziegler
7. Advances in Biophysics, Vol 18, 15
8. Molecular and Cellular Biophysics, Meyer B Jackson (2006), Cambridge)
9. Text Book of Physiology, Guyton & Hall, 11th Ed. 2006

17
 Annexure A

Additional Book for References

Access Title of the Book The Author’s Name

No.
1 Principal of biostatistics 2eld Pagno
2 DNA Micro arrays : a molecular cloning manual Browtell
3 Introduction to protein structure 2eld Branden
4 Guidebook on molecular modeling in drug design cohen
5 Electrophoresis Desai
6 Radioactive releases in the environment copper
7 An Intro. To biomechanics. Humphrey
8 Biophysics : An Intro cotterill
9 Principal of fluorescence spectroscopy 3 eld lokowicz
10 Protein targeting transport and translocation Dalbey
11 Practical protein crystallography 2eld MC.Ree
12 Molecular genetics of bacteria 4eld Dale
13 Biophysics pattabhi
14 Biophysical aspects pf transmembrane Damjanovich
15 Drug discovery and development Rang
16 Textbook of Biophysics Roy
17 A short intro to biomedical engineering Sarbadhikari
18 Practical capillary electrophoresis 2 eld. Weinberger
19 Essential pf genomics and bioinformatics sensen
20 Biophysics subramaniam
21 Protein structure & predication Tramontano
22 Bioinformatics of Genome Regulation and structure Kolchanov
23 Essential bioinformatics Xing
24 Introduction to Bioinformatics Lesk
25 Introduction to Bioinformatics Attwood
26 Functional Genomics hunt
27 Bioinformatics Technologies Chen
28 Micro array Bioinformatics Stekel
29 Basic Biostatistics and its App. Datta
30 Quanti Protein by mass Sep.Euro Sechi
31 Vides Gene.Reg. and Met Collada
32 Essential of biophysics Narayanan
33 Micro for an integrative genomics Kohane
34 Physical chemistry for the Biomedical science Logan
35 Structural biology Teng/Springer
36 Water and the cell Pollack/springer
37 NMR‐MPI USR & moss Bauer spectroscopies in molecular Lascialfari‐Springer
magnets
38 Modeling in molecular biology Cio banu‐springer
39 Chemical Biophysics, Quantitative Analysis of cellular system Beard

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