Buffers (their use in study of biomolecules), pH, pKa of aminoacids, D and L amino acid nomenclature. (2)
Proteins: protein sequencing by chemical and mass & NMR spectroscopic methods, Use of spectroscopic tools in studying bimolecules.
Primary (single letter amino acid codes), Ramachandran plot, secondary (alpha-, 310-, Beta-helices, parallel and antiparallel beta-sheets, gamma 1 turns, beta-turns), circular Dichroism of proteins, super-secondary structural motifs, 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)
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)
Nucleic acids: A, B and Z- DNA structures, Method of replication, sequencing of nucleic acids (chemical, dideoxy and fluorescence), Prokaryotic
Transcription, translation, genetic code, genomes, genes, over expression of recombinant proteins, mutagenesis (random and site directed). Polymerase chain reaction (PCR). (9)
Enzymes and their kinetics: Michaelis-Menten kinetics, Reaction order, competitive, un-competitive, non-competitive and irreversible inhibition of enzymes. Effect of pH, temperature on enzymes activity. (4)
Metabolism: Photosynthesis, Calvin's cycle, Glycolysis, Krebs cycle, electron transport, cofactors. (7)