University Of Delhi Biotechnology

Hi buddy I want to do M.Phil. Biotechnology (Interdisciplinary Course) from University of Delhi and for the same here looking for its syllabus , so would you plz tell me from where I can get it ??

[pawan]

As you want here I am giving below University of Delhi M.Phil. Biotechnology (Interdisciplinary Course) program syllabus on your demand :

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, Non-
standard & 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