Dentistry and Dental Prosthodontics

Learning outcomes: - know the structure and function of amino acids, oligopeptides and water-soluble vitamins - know the structure and function of fibrous proteins, myoglobin, hemoglobin and immunoglobulins - know the properties and function of enzymes and their study - know some methodologies of study and characterization of proteins - know structure and function of carbohydrates and the bonds that stabilize the formation of polymers. Assembly of carbohydrates complexes with proteins and lipids - know structure and function of lipids. Storage lipids and lipid components of membranes. Membrane architecture and function. Detailed program Proteins: Amino acids. Classification, properties, acid-base properties, isoelectric point. Peptide bond, structure and properties. Ramachandran plot. Glutathione, Neuropeptides: vasopressin, oxitocin (overall structure and function). Overall structure and maturation of insulin. Structure of proteins: organization levels. Collagen and its maturation, keratin, fibroin. Hemoglobin and myoglobin, structure and function. Fractional saturation plot. Hill’s equation. Cooperativity and its structural basis. Perutz’s stereochemical mechanism. Allosteric effectors (BPG, CO2, H+, Bohr effect). CO2 blood transport. The Monod-Wyman-Changeux model. Hemoglobinopathies. Blood composition. Introduction to proteomics. Protein folding. Chemical and physical denaturants. Chaperones and chaperonines. The hydrophobic effect. Anfinsen’s experiment and Levinthal’s paradox. APP protein. Molecular basis of degenerative diseases caused by misfolding. Immunoglobulins. Classification. Structure. Principles of biochemical methods. Macromolecules purification and characterization methods: chromatography, electrophoresis, spectrophotometry, fluorimetry. SDS-PAGE, isoelectric focusing. Water soluble vitamins.Vitamins B1, B2, B3, B5, B6, B7, B9, B12, C, Vitamin sources and deficiences. Coenzymes. Enzymes. Enzyme nomenclature. General properties of enzymes: rate acceleration, reaction specificity and stereospecificity, regulation. Catalysis and free energy of activation. Acid-base, covalent and metal ion catalysis. Mechanisms of ribonuclease, carbonic anhydrase and serine proteases. Chemical kinetics: rate equation, reaction order, first-order and second-order specific rate constants. Enzyme kinetics: Michaelis-Menten equation. Significance of KM and VMAX (kCAT) and the specificity constant. Rapid pre-equilibrium hypothesis. The steady state regime. Experimental determination of the steady state parameters. Graphical determination of the steady state parameters: Lineweaver-Burk and Eadie-Hofstee (optional) linear transformations. Enzyme inhibition: competitive, uncompetitive, mixed and non-competitive inhibition. Carbohydrates. General properties and classification. Monosaccharides, oligosaccharides and polysaccharides (starch, glycogen, cellulose, chitin). Heteropolysaccharides, glycosaminoglycans and extracellular matrix. Glycoconjugates: proteoglycans, glycoproteins and glycolipids. Triacylglycerols. Structural lipids in membranes: Phosphoglycerides and Sphingolipids. Cholesterol and derivatives. Arachidonic acid and derivatives. Lipids signals, cofactors and pigments The composition and architecture of membranes. Lipid and protein composition. Membrane proteins: integral, peripheral. Mechanisms of transport across membranes. Passive and active transport. Carriers (glucose transporter, chloride-bicarbonate exchanger), channels and pumps (SERCA pumps and Na/K ATPase). Blood clotting - Factors involved in clotting: serine proteases, Ca2+ and phospholipids. Fibrinogen structure and its polymerization. Transglutaminase. Prothrombin and its activation. Vitamin K and its role in Gla-synthesis. Anticoagulants and fibrinolysis

DL Nelson & MM Cox - Lehninger Principles of Biochemistry (7th edition) D. Voet, JG Voet, CW Pratt - Fundamentals of Biochemsitry- Life at the Molecular Level (5th edition)

Learning outcomes: - know the structure and function of amino acids, oligopeptides and water-soluble vitamins - know the structure and function of fibrous proteins, myoglobin, hemoglobin and immunoglobulins - know the properties and function of enzymes and their study - know some methodologies of study and characterization of proteins - know structure and function of carbohydrates and the bonds that stabilize the formation of polymers. Assembly of carbohydrates complexes with proteins and lipids - know structure and function of lipids. Storage lipids and lipid components of membranes. Membrane architecture and function. Detailed program Proteins: Amino acids. Classification, properties, acid-base properties, isoelectric point. Peptide bond, structure and properties. Ramachandran plot. Glutathione, Neuropeptides: vasopressin, oxitocin (overall structure and function). Overall structure and maturation of insulin. Structure of proteins: organization levels. Collagen and its maturation, keratin, fibroin. Hemoglobin and myoglobin, structure and function. Fractional saturation plot. Hill’s equation. Cooperativity and its structural basis. Perutz’s stereochemical mechanism. Allosteric effectors (BPG, CO2, H+, Bohr effect). CO2 blood transport. The Monod-Wyman-Changeux model. Hemoglobinopathies. Blood composition. Introduction to proteomics. Protein folding. Chemical and physical denaturants. Chaperones and chaperonines. The hydrophobic effect. Anfinsen’s experiment and Levinthal’s paradox. APP protein. Molecular basis of degenerative diseases caused by misfolding. Immunoglobulins. Classification. Structure. Principles of biochemical methods. Macromolecules purification and characterization methods: chromatography, electrophoresis, spectrophotometry, fluorimetry. SDS-PAGE, isoelectric focusing. Water soluble vitamins.Vitamins B1, B2, B3, B5, B6, B7, B9, B12, C, Vitamin sources and deficiences. Coenzymes. Enzymes. Enzyme nomenclature. General properties of enzymes: rate acceleration, reaction specificity and stereospecificity, regulation. Catalysis and free energy of activation. Acid-base, covalent and metal ion catalysis. Mechanisms of ribonuclease, carbonic anhydrase and serine proteases. Chemical kinetics: rate equation, reaction order, first-order and second-order specific rate constants. Enzyme kinetics: Michaelis-Menten equation. Significance of KM and VMAX (kCAT) and the specificity constant. Rapid pre-equilibrium hypothesis. The steady state regime. Experimental determination of the steady state parameters. Graphical determination of the steady state parameters: Lineweaver-Burk and Eadie-Hofstee (optional) linear transformations. Enzyme inhibition: competitive, uncompetitive, mixed and non-competitive inhibition. Carbohydrates. General properties and classification. Monosaccharides, oligosaccharides and polysaccharides (starch, glycogen, cellulose, chitin). Heteropolysaccharides, glycosaminoglycans and extracellular matrix. Glycoconjugates: proteoglycans, glycoproteins and glycolipids. Triacylglycerols. Structural lipids in membranes: Phosphoglycerides and Sphingolipids. Cholesterol and derivatives. Arachidonic acid and derivatives. Lipids signals, cofactors and pigments The composition and architecture of membranes. Lipid and protein composition. Membrane proteins: integral, peripheral. Mechanisms of transport across membranes. Passive and active transport. Carriers (glucose transporter, chloride-bicarbonate exchanger), channels and pumps (SERCA pumps and Na/K ATPase). Blood clotting - Factors involved in clotting: serine proteases, Ca2+ and phospholipids. Fibrinogen structure and its polymerization. Transglutaminase. Prothrombin and its activation. Vitamin K and its role in Gla-synthesis. Anticoagulants and fibrinolysis

DL Nelson & MM Cox - Lehninger Principles of Biochemistry (7th edition) D. Voet, JG Voet, CW Pratt - Fundamentals of Biochemsitry- Life at the Molecular Level (5th edition)