Aligarh Muslim University Msc Biotechnology

Hello sir I want to do Msc in Biotechnology from Aligarh Muslim University so would you please tell me does Aligarh Muslim University offer Msc in Biotechnology if yes then please provide me details about this…

[Quick Sam]

Aligarh Muslim University (AMU) was established in 1875, it is a public university, funded by the central government of India

Yes dude, Aligarh Muslim University offer Msc in Biotechnology

Duration: 2 year

Eligibility:
Candidates must have passed Bachelor of Science (BSc) in Biotechnology from recognized university….

Number of Seats : 14

Syllabus:

SEMESTER I
Biochemistry 3 Credits
Unit I
Chemical basis of life; Composition of living matter; Water – properties; pH; ionization
and hydrophobicity; Emergent properties of biomolecules in water; Biomolecular
hierarchy; Macromolecules; Molecular assemblies; Structure-function relationships
Amino acids – structure and functional group properties; Peptides and covalent structure
of proteins; Elucidation of primary and higher order structures; Evolution of protein
structure; Structure-function relationships in model proteins like ribonuclease A;
myoglobin; hemoglobin; chymotrypsin etc.; Tools to characterize expressed proteins.

Unit II
Enzyme catalysis – general principles of catalysis; Quantitation of enzyme activity and
efficiency; Enzyme characterization and Michaelis-Menten kinetics; Relevance of
enzymes in metabolic regulation; activation; inhibition and covalent modification; Single
substrate enzymes

Unit III
Sugars - mono; di; and polysaccharides; Suitability in the context of their different
functions- cellular structure; energy storage; signaling; Glycosylation of other
biomolecules - glycoproteins and glycolipids; Lipids - structure and properties of
important members of storage and membrane lipids; lipoproteins

Unit IV
Biomembrane organization - sidedness and function; Membrane bound proteins -
structure; properties and function; Transport phenomena; Nucleosides; nucleotides;
nucleic acids - structure; diversity and function; sequencing; Brief overview of central
dogma.

Unit V
Bioenergetics-basic principles; Equilibria and concept of free energy; Coupled
processes; Glycolytic pathway; Kreb's cycle; Oxidative phosphorylation; Photosynthesis;
Elucidation of metabolic pathways; Logic and integration of central metabolism; entry/
exit of various biomolecules from central pathways; Principles of metabolic regulation;
Regulatory steps; Signals and second messengers.

Texts/References:
1. V.Voet and J.G.Voet; Biochemistry; 3rd edition; John Wiley; New York; 2004.
2. A.L. Lehninger; Principles of Biochemistry; 5th edition; W.H Freeman and Company;
2004.
3. L. Stryer; Biochemistry; 5th edition; W.H. Freeman and Company; 2002.

Analytical Techniques 3 Credits
Unit I
Basic Techniques Buffers; Methods of cell disintegration; Enzyme assays and controls;
Detergents and membrane proteins; Dialysis; Ultrafiltration and other membrane
techniques Spectroscopy Techniques UV; Visible and Raman Spectroscopy; Theory and
application of Circular Dichroism; Fluorescence; MS; NMR; PMR; ESR and Plasma
Emission spectroscopy

Unit II
Chromatography Techniques TLC and Paper chromatography; Chromatographic
methods for macromolecule separation -Gel permeation; Ion exchange; Hydrophobic;
Reverse-phase and Affinity chromatography; HPLC and FPLC; Criteria of protein purity
Electrophoretic techniques Theory and application of Polyacrylamide and Agarose gel
electrophoresis; Capillary electrophoresis; 2D Electrophoresis; Disc gel electrophoresis;
Gradient electrophoresis; Pulsed field gel electrophoresis

Unit III
Centrifugation Basic principles; Mathematics & theory (RCF; Sedimentation coefficient
etc); Types of centrifuge - Microcentrifuge; High speed & Ultracentrifuges; Preparative
centrifugation; Differential & density gradient centrifugation; Applications (Isolation of cell
components); Analytical centrifugation; Determination of molecular weight by
sedimentation velocity & sedimentation equilibrium methods

Unit IV

Radioactivity Radioactive & stable isotopes; Pattern and rate of radioactive decay; Units
of radioactivity; Measurement of radioactivity; Geiger-Muller counter; Solid & Liquid
scintillation counters (Basic principle; instrumentation & technique); Brief idea of
radiation dosimetry; Cerenkov radiation; Autoradiography; Measurement of stable
isotopes; Falling drop method; Applications of isotopes in biochemistry; Radiotracer
techniques; Distribution studies; Isotope dilution technique; Metabolic studies; Clinical
application; Radioimmunoassay

Unit V
Advanced Techniques: Protein crystallization; Theory and methods; API-electrospray
and MADI-TOF; Mass spectrometry; Enzyme and cell immobilization techniques; DNA &
Peptide Synthesis.

Texts/References:
1. Freifelder D.; Physical Biochemistry; Application to Biochemistry and Molecular Biology;
2nd Edition; W.H. Freeman & Company; San Fransisco; 1982.
2. Keith Wilson and John Walker; Principles and Techniques of Practical Biochemistry; 5th
Edition; Cambridge University Press; 2000.
3. D. Holme & H. Peck; Analytical Biochemistry; 3rd Edition; Longman; 1998.
4. R. Scopes; Protein Purification - Principles & Practices; 3rd Edition; Springer Verlag;
1994.
5. Selected readings from Methods in Enzymology; Academic Press.

Biostatistics & Computer Applications 3 Credits
Unit I
Fundamental concepts in applied probability; Exploratory data analysis and statistical
inference; Probability and analysis of one and two way samples; discrete and continuous
probability models; Expectation and variance; Central limit theorem; Inference;
Hypothesis; Critical region and error probabilities; Tests for proportion; Equality of
proportions; equality of means of normal populations(variance known; variance
unknown); Chi-square test for independence; P-value of the statistic; Confidence limits;
Introduction to one way and two-way analysis of variance; Data transformations

Unit II
Elements of programming languages - C and PERL; Data base concept; Database
management system; Database browsing and Data retrieval; Sequence database and
genome database; Data Structures and Databases; Databases such as GeneBank;
EMBL; DDBJ; Swissplot; PIR; MIPS; TIGR; Hovergen; TAIR; PlasmoDB; ECDC;
Searching for sequence database like FASTA and Blast algorithm.

Unit III
Cluster analysis; Phylogenetic clustering by simple matching coefficients; Sequence
Comparison; Sequence pattern; Regular expression based pattern; Theory of profiles
and their use in sequence analysis; Markov models; Concept of HMMS; Baum-Welch
algorithm; Use of profile HMM for protein family classification; Pattern recognition
methods

Unit IV
Goals of a Microarray experiment; Normalization of Miroarray data; Detecting differential
gene expression; Principle component analysis; Clustering of microarray data; Structure
determination by X-ray crystallography; NMR spectroscopy; PDB(Protein Data Bank)
and NDB(Nucleic Acid Data Bank); File formats for storage and dissemination of
molecular structure.

Unit V
Methods for modeling; Homology modeling; Threading and protein structure prediction;
Structure-structure comparison of macromolecules with reference to proteins; Force
fields; Molecular energy minimization; Monte Carlo and molecular dynamics simulation
Practicals:
Introduction to MSEXCEL-Use of worksheet to enter data; edit data; copy data; move
data. Use of in-built statistical functions for computations of Mean; S.D.; Correlation;
regression coefficients etc. Use of bar diagram; histogram; scatter plots; etc. graphical
tools in EXCEL for presentation of data. Introduction to SYSTAT package. Searching
PubMed ; Introduction to NCBI; NCBI data bases; BLAST BLASTn; BLASTp; PSIBLAST;
Sequence manipulation Suite; Multiple sequence alignment; Primer designing;
Phylogenetic Analysis. Protein Modeling; Protein structure Analysis; Docking; Ligplot
interactions.


Contact detail:
Aligarh Muslim University
Aligarh, Uttar Pradesh

Map;
[MAP]Aligarh Muslim University[/MAP]
Rest of the syllabus here I am attaching pdf file which is free for download…