Introduction of lipid micelles, monolayers and bilayers
Unit 4 Proteins
14 lectures
Functions of proteins
Primary structure of proteins: Amino acids as building blocks
General formula of amino acid and concept of zwitterion
Titration curve of amino acid and its significance
Classification, biochemical structure and notation of standard protein amino acids
Ninhydrin reaction
Natural modifications of amino acids in proteins: hydrolysine, cystine, hydroxyproline
Non-protein amino acids: Gramicidin, beta-alanine, D-alanine and D-glutamic acid
Oligopeptides: structure and functions of glutathione, insulin and synthetic aspartame
Secondary structure of proteins: Peptide unit and its features, alpha helix, beta pleated sheet
Tertiary and quaternary structures of proteins
Forces holding the polypeptide together
Human haemoglobin structure
Quaternary structures of proteins
Unit 5 Enzymes
12 lectures
Structure of enzyme: Apoenzyme and cofactors
Prosthetic groups: TPP, coenzymes like NAD, metal cofactors
Classification of enzymes
Mechanism of enzyme action: active site, transition state complex and activation energy
Lock and key hypothesis and Induced Fit hypothesis
Significance of hyperbolic and double reciprocal plots of enzyme activity
Km and allosteric mechanisms
Definitions: enzyme unit, specific activity and turnover number
Multienzyme complex: pyruvate dehydrogenase
Isozyme: lactate dehydrogenase
Effect of pH and temperature on enzyme activity
Enzyme inhibition: competitive inhibition by sulfa drugs and non-competitive inhibition by heavy metal salts
This Biochemistry course provides a foundational understanding of the chemical principles underlying biological processes. It covers the thermodynamic basis of metabolism, including the laws of thermodynamics, Gibbs free energy, and energy coupling in biochemical reactions. Students will explore the structure, classification, and biological roles of key biomolecules including carbohydrates, lipids, proteins, and enzymes.
The course introduces monosaccharides, disaccharides, and polysaccharides with a focus on structural variations and functional relevance. It examines lipid classes such as fatty acids, phospholipids, and sphingolipids, highlighting their significance in energy storage, membrane structure, and signaling. In the protein section, learners study amino acid chemistry, peptide formation, and protein folding, with detailed analysis of structural levels and functional proteins like hemoglobin.
Enzymology covers enzyme classification, catalytic mechanisms, kinetics, inhibition, and regulatory behavior, supported by graphical analyses and model systems. Real-world biochemical systems such as multienzyme complexes and metabolic enzymes are discussed to connect theory with application.
This course equips students with critical biochemical concepts essential for advanced studies in molecular biology, biotechnology, physiology, and related life sciences disciplines.
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