Peptides and Proteins
Course Feature
Class Description
Functional groups of biomolecules. Intermolecular interactions. Charged and neutral molecules. Hydrogen bonding. Hydrophobic interactions. Structural features conferring water solubility. Amino acids: natural, proteinogenic, non-natural. Acidity and basicity. pKa. Henderson-Hasselbach equation. Peptide bond. Peptide bond formation. Determination of peptides charge. Proteins: composition and structure. Chemical properties, electric charges. Primary structure. Higher organization levels. Folding and protein stability. Nature and role of non-covalent interactions. Inter- and intra-molecular bonds and biological properties. Cross-linking. Disulphide bonds. Methods to determine protein structure. Structural and fibrous proteins. Collagen, elastin, keratins, silk proteins. Myosin, actin, movement. Molecular machines analogues of natural elastin. Globular proteins: myoglobin, haemoglobin (Hb). Oxygen transport. Hill number. Bohr effect. Hb of type R- and T-. Sickle cell anemia. Structure activity relationship. Antibodies. Enzymes. Catalysis. Protein families with a common catalytic mechanism: serine proteases. Enzyme kinetics. Inhibition. Regulation of enzymatic activity. Analytical applications of enzymes. Enzyme classes and their application in biocatalysis. Hydrolases, lyases, ligases, kinases. Membrane proteins. Transport mechanism of charged or un-charged species. Active or passive transport. Aquaporin. Ionic channels. Thermodynamics of sequential transformations. Systems using or producing energy. Thermodynamic of high energy content transforming compounds.
Final examination: written examination in a multiple-choice test of 16 sets, conceptual or numerical exercises.
Didactic material: (slide show in english)
Suggested reading: David Whitford, Proteins: Structure and Function, Editor: John Wiley & sons, Ltd, 2005, ISBN: 978-0471-49894-0 Note: No italian version of this book. Contains at least 60% of the lesson topics
