Learning objectives
<br />The student will, in the first place, become familiar with the structure and manyfold functions of proteins, learning about the fundamental role of these molecules in cellular processes. Furthermore, the student will be introduced to the main classes of small molecules (sugars, lipids, amino acids and nucleotides) that occur in living organisms. The course will examine the metabolic pathways leading to the degradation and biosynthesis of these molecules in the cell, as well as the mechanisms for the production and use of metabolic energy.
Prerequisites
<br />Pre-requisites (strongly recommended): courses in Mathematics, General & Inorganic Chemistry, Organic Chemistry.
Course unit content
<br /> Proteins: structure and function<br />Amino acids. The peptide bond. The three-dimensional structure of proteins: primary, secondary, tertiary and quaternary structures. Protein function and evolution. Hemoglobin: a model allosteric protein. Enzymes: basic concepts and kinetics. The Michaelis-Menten model. Enzyme inhibition. A paradigmatic enzyme: chymotrypsin. Regulation of enzyme activity. Membrane proteins and the structure of biological membranes.<br />Metabolism<br />Fundamentals of bioenergetics: DG0 and DG0’. ATP, a ready-to-use source of chemical energy. Other key molecules in metabolism: NADH, FADH2, coenzymes and vitamins. Carbohydrates: definition, description and main chemical features. Glycolysis and fermentations. The citric acid cycle. The pentose-phosphate pathway. Gluconeogenesis and glycogen metabolism. Oxidative phosphorylation in the mitochondria: the electron transport chain, the creation of proton gradients and the biosynthesis of ATP. Fatty acid metabolism: beta-oxidation and biosynthesis. Ketone bodies. Degradation of the amino acids and the urea cycle. Nitrogen fixation. The biosynthesis of amino acids and nucleotides.<br />How proteins are studied (laboratory exercises) <br />Protein purification. Chromatography techniques: size exclusion, ion exchange, and affinity chromatography. Protein electrophoresis. Spectrophotometric techniques for the study of proteins and enzymes.
Full programme
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Bibliography
<br />David L. Nelson e Michael M. Cox<br />I Principi di Biochimica di Lehninger (3rd Ed.)<br />Zanichelli, Bologna, 2002<br /><br />Donald Voet, Judith G. Voet e Charlotte W. Pratt<br />Fondamenti di Biochimica<br />Zanichelli, Bologna, 2002<br /><br />Mary K. Campbell, Shawn O. Farrell<br />Biochimica<br />EdiSES, Napoli, 2004
Teaching methods
<br />The course includes both formal classes and laboratory exercises.<br />During formal classes, the teacher will illustrate – also with the support of audiovisual material - the properties of proteins and enzymes, as well as the main metabolic pathways. <br />During laboratory hours, the students will learn and practice the main techniques used in the laboratories of biochemistry - techniques aimed at the identification, purification and functional characterization of proteins. <br />The final assessment of the students will be based on a written examination.
Assessment methods and criteria
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Other information
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