Department of Biotechnology - SGBAU

This course comprises of 6 Units.

Unit I

Proteins and Amino Acids (8 periods)

Amino acids: Classification, properties, peptide bond,

Proteins: Classification and function, evolution of protein structure, Protein folding: Anfinsen’s Dogma, Levinthal paradox, cooperativity in protein folding, free energy landscape of protein folding and pathways of protein folding, molten globule state, chaperons, diseases associated with protein folding. Introduction to molecular dynamic simulation. Protein degradation and introduction to molecular pathways controlling protein degradation, structure-function relationships in model proteins like ribonuclease A, myoglobin, haemoglobin, chymotrypsin etc.; Anabolism and catabolism of Amino Acids.

Unit II

Enzymes as Biocatalysts (8 periods)

International classification of enzymes. Enzyme Kinetics; Methods for measuring kinetic and rate constants of enzyme reactions and their magnitudes, Inhibitors. Isozymes Enzyme turnover: methods of its measurements and significance

Allosteric enzymes, sigmoidal kinetics and their physiological significance. Symmetric and sequential modes for action of allosteric enzymes, negative and positive cooperativity, General mechanisms of enzyme regulation: Feedback inhibition and feed forward stimulation, enzyme repression, induction and degradation, control of enzyme activity by products and substrates;

Co-enzymes and cofactors: Water soluble vitamins and their co-enzymes, metalloenzymes. Ribozymes and abzymes, Enzymes as druggable targets.

Unit III

Carbohydrates (8 periods)

Carbohydrates: Glycolysis and TCA cycle; Glycogen breakdown and synthesis; Gluconeogenesis; Inter-conversion of hexoses and pentoses; Mitochondrial respiratory chain: Organization of carrier, proton gradient, iron sulphur proteins and cytochromes. Reversed electron transfer, respiratory controls and oxidative phosphorylation, uncouplers and inhibitors of energy transfer ATP: Synthetase complex, microsomal electron transport, partial reduction of oxygen, superoxides ATP cycle and cell bioenergetics.

Unit IV

Classification (simple, compound and derived lipids), Structure, function and their industrial significance, Oxidation of lipids; Biosynthesis of fatty acids; Triglycerides; Phospholipids; Glyco and Lipoproteins, Sterols, membrane lipids and lipid rafts, Circulating lipids with relevance to pathological changes.

Unit V

Nucleic Acids: (7 periods)

Nucleotides, types and structures, their synthesis, de novo and salvage pathway, Regulation of pathways.

Structure of DNA: A, B and Z forms.

Unit VI

Techniques (7 periods)

Basic principles of protein purification; tools to characterize expressed proteins. Sequencing of proteins, Sanger-Edman, MS-ESI, MALDI-TOF, Physical and chemical methods for study of Protein-protein and protein-ligand interactions. and sequencing of nucleic acids. Dideoxy, automated, Nanopore, Ion torrent, Illumina