|1||Title of the course |
|3||Course content||Major classes of biological molecules: Comparison of the alphabets and sources of structural diversity of proteins, nucleic acids, carbohydrates and lipids. |
Proteins : Ramachandran plot, evolution of protein structure, structure-function relationships: myoglobin and adaptions in myoglobin structure in deep diving mammals; allostery in hemoglobin; Bohr effect (for pH and carbon dioxide); adult and foetal hemoglobin. Post-translational modifications: special types of covalent bonds found in proteins. Protein folding: Natively folded and natively disordered proteins; miniproteins and peptine toxins; Anfinsen's observations, Levinthal paradox, cooperatively in protein folding; free energy landscape of protein folding and pathways of protein folding, molten globule state, diseases associated with protein folding.
Carbohydrates: Sources of structural diversity; structure-function relationship in glycogen and celllose, Difficulty associated with sequencing of glycans.
Lipids : Structure and properties of storage and membrane lipids. Self-assembly of lipids:packing parameter; Biomembrane organization-sidedness and function; membrane bound proteins - structure, properties and function; transport phenomena.
Nucleic acids : Historical perspective leading up to the proposition of DNA double helical structure of RNA; chromatin organization.
Enzymes: General principles of catalysis; quantitation of enzyme activity and efficiency; Henri-Michaelis-Menten and Briggs-Haldane relationships; Transition state: definition Pauling's intuition and proposal, catalytic antibodies; Catalytic strategies; Isozymes : Haldane relationship between kinetic constants and equilibrium constant; Zymogens.
Bioenergetics: basic principles; equilibria and concept of free energy; coupled interconnecting reactions in metabolism; oxidation of carbon fuels; recurring motifs in metabolism. Relevant metabolic pathways may be included to discuss relevant concepts.