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Course Contents

Buffers (their use in study of biomolecules), pH, pKa of amino acids, D and L amino acid nomenclature. (1)Proteins: protein sequencing by chemical and mass & NMR spectroscopic methods, Use of spectroscopic tools in studying biomolecules. Primary (single letter amino acid codes), Ramachandran plot, secondary ®-, 310-,  ¼-helices, parallel and antiparallel ¯-sheets, ¯-turns, °-turns), circular dichroism of secondary structures, tertiary (motifs and domains : some important motifs like Rossman fold, helix turn helix, 4 helix bundles, beta barrel) and quaternary structure (Hemoglobin and Myoglobin). Protein Engineering (17).Nucleic  acids: A, B and Z-DNA structures, Method of replication, sequencing of nucleic acids (chemical, dideoxy and fluorescence), Transcription, Translation, genetic code, genomes, genes, over expression of recombinant proteins, mutagenesis (random and site directed). Polymerase chain reaction (PCR). Use of modified bases in PCR   (9)Carbohydrates and Glycoproteins, proteoglycans, Membranes and lipids, bacteial cell wall synthesis and mechanism of some important antibiotics like penicllin, antibiotic resistance. (4)Metabolism: Photosynthesis, Calvin’s cycle, Glycolysis, Krebs cycle, electron transport, cofactors. (4)Enzymes and their kinetics: Michaelis-Menten kinetics, Reaction order, competitive, un-competitive, non-competitive and irreversible inhibition of enzymes. Effect of pH, temperature on enzyme activity. (4)Biophysical techniques to purify and study proteins. Dialysis, salting out and precipitation by organic solvents, Ion exchange, gel filtration, reversed phase, affinity chromatography, ultracentrifugation, gel electrophoresis. (3)



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  1. Fundamentals of Biochemistry by Voet, Voet and Pratt,
  2. Biochemistry by L. Stryer,
  3. Proteins by T.E. Creighton,
  4. Genes VII by B. Lewin,
  5. Introduction to protein structure by Branden and Tooze,
  6. Enzyme structure and Mechanism by Alan Fersht.



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