Unit CHEMISTRY AND BIOCHEMISTRY I

BIOCHEMISTRY I - MOD. 1

Code	GP004762
CFU	3
Teacher	Ilaria Bellezza
Teachers	Ilaria Bellezza
Hours	37.5 ore - Ilaria Bellezza
Learning activities	Base
Area	Struttura, funzione e metabolismo delle molecole d'interesse biologico
Academic discipline	BIO/10
Type of study-unit	Obbligatorio (Required)
Language of instruction	Italian
Contents	Structural biochemistry: carbohydrates, lipids, nucleotides, nucleic acids, amino acids, proteins. Hemoglobin and myoglobin
Reference texts	I principi di Biochimica del Lehninger - Nelson, Cox, Zanichelli Biochimica Berg, Tymoczko, Stryer Zanichelli Biochimica Medica Siliprandi, Tettamanti Piccin
Educational objectives	The main competence will be to have a general knowledge necessary to address the lessons of Module 2.
Prerequisites	The student must have acquired basic knowledge of the main topics of General Chemistry and Organic Chemistry
Teaching methods	The course is organized in frontal lessons and theoretical practical lessons
Other information	The attendance is compulsory at least 70% of lessons. Terni–School of Medicine – Educational and Scientific Center
Learning verification modality	The final exam consists of a written test and an oral exam. The written test consists of 30 multiple-choice questions relating to any topic covered in the course. For each question 4 possible answers are available of which only one is always program. Each question is awarded 1 mark if answered correctly and 0 marks if answered incorrectly. The minimum mark for passing the written test is 18/30. Passing the written test is compulsory for access to the oral exam but its evaluation does not contribute to the definition of the final mark. The oral examination, lasting an average of 30 minutes, will cover all the topics discussed during the course. Knowledge of the chemical formulae of the metabolites, enzymatic reactions and their regulation are required. During the oral examination, the student's ability to critically link different topics and the ability to express himself/herself in precise and clear technical language will be assessed.
Extended program	Monosaccharides, monosaccharide cyclization, monosaccharide reactions, glycosidic bonding, oligosaccharides (sucrose, lactose, maltose), polysaccharides (glycogen, starch, cellulose, inulin), glycosaminoglycans (ac. hyaluronan, heparan sulfate, dermatan sulfate, chondroitin sulfate), Glycoconjugates (glycoproteins, proteoglycans, glycolipids). Nucleotides, Nucleosides, phosphodiester binding, DNA-RNA stability, DNA structure, RNA structure, DNA-RNA differences, ATP functions. Fatty acids (nomenclature, structure and properties), triacylglycerols (structure and properties), glycerophospholipids (structure and properties), dipalmitoylphosphatidylcholine, cardiolipin, glycerophosphatidylinositol, sphingolipids (sphingomyelins, gangliosides), sterols, isoprenoid derivatives, arachidonic acid derivatives. Amino acids (structure and properties), amino acid titration curves, peptide bonding (structure and properties), secondary structures: alpha-helix, sheet-beta, beta turn (structure and properties), three-dimensional structure of proteins and bonds that stabilize it. Fibrous proteins. Collagen: structure, function, post-translational modifications, hydroxylation of Pro and Lys, cross-links, collagen-associated diseases, role of vitamin C. Alpha-keratin (structure and function), myosin (structure and function). Structural motifs (helix-loop-helix, leucine zipper, zinc finger), structural domains (TIM barrel, head-tail barrel, beta sandwich), quaternary structure. Folding: thermodynamics, kinetics, protein aggregation, HSP (60, 70, 90), protein disulfide isomerase, peptidyl-prolyl isomerase. Hemoglobin and myoglobin. Heme group (structure hints, polypeptide chain binding, function), myoglobin structure, saturation curve, myoglobin structure, conformational states, saturation curve, allosteric modulators (O2, CO2, H+, 2,3, BPG). CO2 transport. HbF, HbS, methemoglobinemia. Actin and myosin, structure, mechanism of muscle contraction.
Obiettivi Agenda 2030 per lo sviluppo sostenibile

BIOCHEMISTRY I - MOD. 2

Code	GP004764
CFU	3
Teacher	Ilaria Bellezza
Teachers	Ilaria Bellezza
Hours	37.5 ore - Ilaria Bellezza
Learning activities	Base
Area	Struttura, funzione e metabolismo delle molecole d'interesse biologico
Academic discipline	BIO/10
Type of study-unit	Obbligatorio (Required)
Language of instruction	Italian
Contents	The Module 2 program covers the following topics: Enzymes. Coenzyme structure and mechanism of action. Biological membranes. Signal transduction. Catabolism and Anabolism. Bioenergetics. High-energy bonds. ATP. Respiratory chain and oxidative phosphorylation
Reference texts	I principi di Biochimica del Lehninger - Nelson, Cox, Zanichelli Biochimica Berg, Tymoczko, Stryer Zanichelli Biochimica Medica Siliprandi, Tettamanti Piccin
Educational objectives	At the end of the course the student should be in possession of the main knowledge related to Structural Biochemistry, Functional Biochemistry and Energy Biochemistry
Prerequisites	The student must have acquired basic knowledge of the main topics of General Chemistry and Organic Chemistry and Structural Biochemistry
Teaching methods	The course is organized in classroom theoretical lessons
Other information	The attendance is compulsory at least to 70% of classes. Terni School of Medicine – Educational and Scientific Center
Learning verification modality	The final examination consists of a written test and an oral exam. The written test consists of 30 multiple-choice questions relating to any topic covered in the program. For each question 4 possible answers are available of which only one is always correct. The answer is deemed to be correct when only the single correct choice is selected from those present. Each question is awarded 1 mark if answered correctly and 0 marks if answered incorrectly. The minimum mark for passing the written test is 18/30. Passing the written test is compulsory for access to the oral exam but its evaluation does not contribute to the definition of the final mark. The oral examination, lasting an average of 30 minutes, will cover all the topics discussed during the course. Knowledge of the chemical formulae of the metabolites, enzymatic reactions and their regulation are required. During the oral examination, the student's ability to critically link different topics and the ability to express themselves in precise and clear technical language will be assessed.
Extended program	Enzymes: characteristics, classification, active site, thermodynamics of catalyzed reactions, activation energy, binding energy, induced adaptation, factors affecting speed of reactions (pH, T, [S]), enzyme kinetics (Michaelis-Menten kinetics), kinetic parameters, multi-substrate reactions, enzyme inhibition (irreversible inhibitors, competitive, incompetitive and mixed inhibitors). Catalytic mechanisms: acid-base catalysis (e.g. ), metal ion catalysis (e.g. carbonic anhydrase, enolase, aconitase), covalent catalysis (e.g. aldolase), serine protease (catalytic mechanism, induced adaptation, intermediate stabilization, substrate specificity). Allosteric modulators. Reversible covalent modifications (e.g., phosphorylation), irreversible covalent modifications (e.g., limited proteolysis). Protein half-life regulation (e.g., ubiquitin-proteasome). Vitamins and coenzymes: ac. ascorbic (structure and function), thiamine (structure and coenzyme mechanism), ac. lipoic acid (structure and coenzyme mechanism), riboflavin (structure and coenzyme mechanism), niacin (structure and coenzyme mechanism), pantothenic acid (hints at structure and coenzyme function), pyridoxine (structure and coenzyme mechanism), Biotin (structure and coenzyme mechanism), folic acid and vitamin B12 (hints at structure and coenzyme function). Hints of function of fat-soluble vitamins (A,K,D, E). Pyruvate dehydrogenase complex (structure, catalytic maccanism, regulation). Biological membranes: asymmetry, fluidity, fluid mosaic model, transmembrane proteins (structural properties). Membrane transport: thermodynamics of transport, simple diffusion, facilitated transport (Glut, chloride bicarbonate exchanger, K+ channel, aquaporins), primary active transport (Na+/K+ pump, SERCA pump, ABC transporters), secondary active transport. Biosignaling: characteristics, GPCR receptors (Gs, Gi, Gq) signal transduction and switching off, receptor tyrosine kinase mechanism of action and signal switching off, GMPcyclic, NO, second messengers derived from phosphatidylcholine and sphingomyelin, receptors for steroid hormones mechanism of action. Bioenergetics: general characteristics of metabolism (catabolism and anabolism), thermodynamics of metabolism, energy function of ATP, other roles of ATP, Substrate-level phosphorylation (1,3, bisphosphoglycerate, phosphocreatine, phosphoenolpyruvate, succinylCoA), thermodynamic aspects; oxidative phosphorylation: Oxidoreduction reactions, carbon oxidation states, chemiosmotic theory, electron transport chain 8structure and function of complexes), reactive oxygen species, oxidative stress and antioxidant defenses (GSH), chemiosmotic coupling, ATP synthase (structure and mechanism of rotational catalysis), thermodynamic and quantitative aspects, malate aspartate shuttle, glycerol 3-phosphate shuttle, regulation of oxidative phosphorylation, uncoupling agents.
Obiettivi Agenda 2030 per lo sviluppo sostenibile

CHEMISTRY - MOD. 1

Code	GP004761
CFU	3
Teacher	Davide Chiasserini
Teachers	Davide Chiasserini
Hours	37.5 ore - Davide Chiasserini
Learning activities	Base
Area	Struttura, funzione e metabolismo delle molecole d'interesse biologico
Academic discipline	BIO/10
Type of study-unit	Obbligatorio (Required)

CHEMISTRY - MOD. 2

Code	GP004763
CFU	2
Teacher	Davide Chiasserini
Teachers	Davide Chiasserini
Hours	25 ore - Davide Chiasserini
Learning activities	Affine/integrativa
Area	Attività formative affini o integrative
Academic discipline	BIO/10
Type of study-unit	Obbligatorio (Required)