Course contents *
Biophysical chemistry: Amino acid conformations & properties, Ramachandran plots. Hydrogen bonds. Thermodynamics, entropy, free energy, and hydrophobic interactions. Electrostatics in biomolecules and solution, disulphide bonds. Properties of polypeptide chains. Alpha, 3-10, and Pi-helices. Parallel and anti-parallel beta sheets. Turns and loops. Conformational changes, helix-coil transitions, stability of secondary structure elements in water and other solvents. Non-polar, polar, and charged amino acid side chains.
Protein structure: Packing of helices and sheets, supersecondary structure. Collagen, keratin, silk, and other simple structures. Structure and function of water-soluble proteins, classification of protein folds. Protein aggregation/misfolding, prions (mad cow disease). Membranes and membrane proteins. Evolution and natural selection of structures.
Protein folding & structure prediction: Anfinsen's Hypothesis. Levinthal's paradox. Kinetics of protein folding. Two-state folding and intermediates. Molten globule or folding nuclei. Energy landscapes. Pathways. Prediction of structure from amino acid sequence. Threading.
Protein function: Docking and binding. Enzyme function. Active sites. Induced fit. Specificity and allostery. Membrane protein function. Protein engineering and design.