Course Content (Syllabus)
Introduction. Chemistry of Amino acids, peptides and proteins. Geometry of peptide bond, coupling of amino acids-methods of peptide synthesis. Protection of amino, carboxyl and of other functional groups of amino acids.
Solid phase and solution synthesis of peptides. Protein conformation, physicochemical properties of proteins. Denaturation. Methods for purification, isolation and identification of proteins. Classification of proteins. Enzymes: General Catalysts: Homogeneous and heterogeneous catalysis, enzymes, Enzyme specifications, nomenclature, coenzymes. Hydrolytic Enzymes-applications. Non-hydrolytic enzymes and their applications. Kinetics of Enzyme reactions –equations. Effect of pH and temperature. Enzyme Inhibitors: multiple substrates – Competitive and non competitive inhibition. Equations-Examples.
Enzyme immobilization: methods of immobilization (molecular and ion bonding, adsorption, entrapment, copolymerization)
Enzyme models: general – Host and guest theory. Ion-phores, Polymers and Cyclodextrins.
Enzyme production from animal, plant, cells and microorganisms. Biotransformation, microbial production of chemicals, vitamins, sugars, steroids, antibiotics.
Chemistry of Nucleic Acids: structure, (primary and secondary conformation). DNA denaturation. Nucleosides and nucleotides. Nomenclature and symbols. Chemical reactions of nucleic acids. Chemical synthesis of oligo- and polynucleotides. Some well known nucleotides and their biological role. DNA and RNA replication. Genetic code. Protein biosynthesis.
Chemical modification of proteins. New syntheses. Solid state reactions. Solvent free reactions. Products with applications to Biomedicine and Pharmaceutics.
Keywords
Enzymes, Proteins, Solid state reactions, Solvent free reactions, New synthesis