Delhi University Biotechnology admission

I want to get admission in M.Phil. Biotechnology in University of Delhi and for that I want to get the details of eligibility criteria so can you provide me that?

[Shaleen]

As you want to get the eligibility criteria to get admission in M.Phil. Biotechnology in University of Delhi so here is the information of the same for you:

Duration:
2 Semester

Eligibility for Admission:
Candidates must have passed M.Sc. in Microbiology/Biotechnology/Life Science from UGC recognized University.

Candidates must have at least 58% in M.Sc. level.

Student should have financial support through NET or any other source.

Selection Process:
Selection will be on interview basis.

No. of Seats:
6

Syllabus:
Semester 1:
Proteins – Structure, Folding and Engineering
Cell Biology – I
Membrane Biology
Molecular Biology -I
Recombinant DNA Technology and Applications - I
Applications of Proteomics and Metabolomics
Developmental Biology

Semester 2:
Enzymes and Techniques in Biochemistry
Cell Biology -II (Cellular Signalling)
Immunology and Immunotechniques
Molecular Biology – II
Recombinant DNA Technology and Applications – II

Proteins – Structure, Folding and Engineering:
1. Introduction:
Genesis; History; Importance and Significance of proteins; Functional diversity, Ubiquity, Classes and Dynamism; Structure-function relationship; Key Features.

2. Amino acids as constituents:
Acid/Base properties, Bifunctional monomers, Polarity, Classification,
Chirality & Stereochemistry, pKa, Codes, Ways of representation, Essential, Non-essential, Nonstandard & Non-proteinogenic amino acids.

3. Physico-chemical interactions in biological systems:
Covalent & non-covalent interactions, Importance of water, Accessible surface area, Importance of weak interactions.

4. Levels of protein structure:
Primary structure: Importance of amino acid sequence, Peptide bond and polypeptide – polarity, direction, backbone and side chains, Importance of H-bonding, Cross-linking in polypeptides, Flexibility and conformational restrictions, Characteristics of peptide bond, Trans- and cis-peptide bonds, Rotation of adjacent peptide bonds, Dihedral angles – phi and si, Ramachandran
plot, Thermodynamic considerations. Secondary structure: H-bonding scheme, Alpha-helices, Screw sense, Diversity in alpha-helices, Alpha-helical wheel, Helix capping, Beta-stand and sheet, Types of beta-sheet, Ramachandran plots, Turns and loops, Importance of loops. Tertiary structure: General properties and characteristics, Myoglobin structure as model, Supersecondary structures, Protein Data Bank (PDB). Quaternary structure: Concept of subunits and protomers, Kinds of subunit association, Importance of quaternary structure, Various examples.

5. Fibrous and Globular proteins, Structural Features of Membrane proteins

6. Protein Classification and Structure Prediction:
Importance, Assumptions, Classes and Databases; Terminologies like domains, motifs, folds, architecture, active site, Examples; Secondary structure prediction; Theories and tools; Tertiary structure prediction (Modeling).

7. Protein Folding: Genesis and definition;
The “protein folding problem”; Terminologies; Denaturants and their mode of action; Anfinsen’s classical experiment; Propensities of amino acids to form secondary structure; Folding curves and transitions; Cooperative protein folding; Equilibrium and kinetic intermediates; Models and Theories of protein folding; Assisted protein folding (Chaperones); Misfolding and diseases; Current status.

8. Protein Engineering:
Basic principles; Types and Methods; Strategies in protein engineering (Directed evolution, Comparative design, Rational design); Applications.

9. Solvent Engineering, Solubility / stability of proteins in solutions:
Interaction of protein, water and solvent; Importance of solvents; Factors affecting aqueous solubility; Physical basis for protein denaturation/ stability; Effect of primary structure on stabilization; Preferential binding and preferential hydration models; Thermodynamics of unfolding; Rationalizing stabilities of folded conformations; Various stabilizers.

10. Techniques to investigate protein conformation and folding:
Spectroscopic methods : Absorbance, Fluorescence, Circular dichroism; Electrophoretic methods : Limited proteolysis and SDS-PAGE, Transverse Urea gradient gel electrophoresis; Hydrodynamic methods : gel filtration, analytical ultracentrifugation; Calorimetric methods – Differential Scanning Calorimetry (DSC); Structural methods : NMR; Mass spectrometry.

Suggested study material
1. D. Sheehan. 2009. Physical Biochemistry: Principles and Applications, John Wiley and Sons Ltd, Chichester, England.
2. C. Branden, T. Tooze. 1999. Introduction to Protein Structure, Garland Publishing, New York, USA.
3. T.E. Creighton. 2002. Proteins: Structures and Molecular Properties, W.H. Freeman and Company, New York, USA.
4. A. M. Lesk. 2004. Introduction to Protein Science: Architecture, Function and Genomics, Oxford University Press, Oxford, England.
5. R. Pain. 2000. Mechanisms of Protein Folding, Oxford University Press, Oxford, England.
6. M. Arai, K. Kuwajima. 2000. Advances in Protein Chemistry, Academic Press, New York, USA.
7. J. Cavanagh, W.J. Fairbrother, A.G. Palmer III, M. Rance, N. J. Skelton. 2007. Protein NMR Spectroscopy: Principles and Practice, Academic Press, San Diego, USA.
8. S. Lutz, U. W. Bornschesser. 2008. Protein Engineering Handbook, Wiley-VCH, Weinheim, Germany.
9. D. W. Mount. 2004. Bioinformatics: Sequence and Genome Analysis, Cold Spring Harbor Laboratory, Plainview, New York, USA.
10. V. N. Uversky, A.L. Fink. 2006. Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein Aggregation and Conformational Diseases (Protein Reviews), Springer, New York, USA.

For more detailed information I am uploading a PDF file which is free to download:


Contact Details:
University of Delhi
University Road
New Delhi,
Delhi 110007
India

[MAP]University of Delhi [/MAP]