Ateneo - UPO

Glucides. Lipids. Amino acids. Structure of proteins. Structure-function relationship of protein. Carrier proteins. Enzymes. Reaction rates. Regulatory mechanisms. Vitamins and cofactors. Reporting Mechanisms. Classes of receptors (Trimeric G protein coupled receptors, Voltage dependent and ligand dependent channels, cADPR and NAADP. PKC. Endocannabinoids, Tyrosine kinase receptors, insulin receptor, receptor-like tyrosine phosphatase, serine / threonine kinase receptors, cGMP signaling -dependent and NO, integrins). Bioenergetics. Cellular respiration. Metabolism.

Biochemistry I & II
• Devlin. Chemistry with clinical aspects.EdiSES
• Siliprandi and Tettamanti. PICCIN Medical Biochemistry.
• Stryer. Biochemistry. Zanichelli.
• Nelson Cox. Lenninger's principles of biochemistry. Zanichelli
• Campbell, Farrel. Edises Biochemistry.
• MARKS. Medical Biochemistry, a clinical approach. Ambrosiana Publishing.

Student acquires the fundamental principles for the understanding of biological mechanisms at the cellular and molecular level, the fundamental and methodological principles of the structure and function of biomolecules, enzymes and enzymatic catalysis, bioenergetics. for the understanding of metabolic regulation and signal transduction mechanisms. The course provides those foundations that will be preparatory to easily follow courses in Physiology, General Pathology, Pharmacology and to initiate students to the experimental approach in the biochemical field. Ability to apply knowledge and understanding: it is expected that the student will be able to apply the knowledge acquired in a multidisciplinary key knowing how to grasp the knowledge in a biochemical key to solve problems also in other courses. Autonomy of judgment: applying learned methods, ability to understand and critically discuss the acquired knowledge; ability to understand and critically discuss the results obtained in the field of biochemical research. Communication skills: demonstrate the ability to communicate effectively both orally and in writing; demonstrate ability to summarize and present information; demonstrate that they are able to communicate and present effectively and objectively, using an adequate scientific language, information and experimental results obtained and to draw the appropriate conclusions from them. Learning skills: ability to read, understand and comment on a scientific text of biochemistry. Acquisition of the ability to critically deepen and update the objectives and / or results of a research plan according to both a quantitative and a qualitative approach.
At the end of the course the student must be able to describe, in molecular terms, the structure of biological matter, knowing how to recognize the role of the structure on the functionality of the macromolecules themselves.
He will also have to show mastery of the main signal transduction mechanisms, knowing how to focus their role in cell signaling processes.

Passing exams in Chemistry.
Attendance of biology and anatomy exams.

Lectures and activity in e-learning platform (DIR); Slides provided by the teacher
Lessons on the elearning platform
Reference websites.
There are frequent self-assessment tests and an on-going assessment test both during lectures and from home.
The DIR site provides a tutorial activity for practice lessons and exercises with correction of the papers.

Learning control: collegial discussion of the topics of the program and of the numerical exercises proposed during the lessons. Course is supported in the web site DIR section with appropriate material to verify the degree of initial preparation and learning “in itinere”. There are traces of discussion and verification of the study of the topics covered in the course. There are also tests with open-ended and multiple-choice questions and numerical exercises for the evaluation of the study. The teacher answers only to e-mail signed and coming from the domain: matricola@studenti.uniupo.it. Students with physical disabilities, Learning Disabilities or Special Education Needs can request specific services and tools via the Staff Sviluppo e Coordinamento Carriere e Servizi alle Studentesse e agli Studenti, consulting the University webpage: https://www.uniupo.it/en/services/services-students-physical-or-learning-disabilities Students with disabilities, learning disabilities or special education needs, once they have contacted the University Staff, can refer to the tutor in charge of the course to define the examination modalities, concerning academic aspects.

Objective of the exam is to verify the level of knowledge and depth of the topics of the course program and the reasoning skills developed by the student. The exam involves passing a written and an oral test on the same day. The written test lasts one hour. Questions in the written test include: multiple choice tests, molecular structures, numerical exercises, open-ended questions, related to all the topics of the course program. The answers to open questions are judged for both content and appropriate language. The scores of the questions are indicated in the assignment. Written exam of Biochemistry 1, the mark remains valid until the month of December of the current academic year. The student with a sufficient grade will be able to sit the oral in the part of Biochemistry 2. The overall assessment will take into account the elements collected by the commission in the written test, including the grade of the molecular biology part and in the oral one During the written test it is not allowed to consult any type of material. The use of the calculator is recommended. The exam allows you to evaluate knowledge (theoretical questions), skills (any exercises), critical sense and learning ability (exercises with a request to express a judgment or to make a choice between different alternatives). Open questions allow you to assess communication skills. The exam allows you to evaluate knowledge (theoretical questions), skills (exercises), critical sense and learning ability (exercises with a request to express a judgment or to make a choice between different alternatives). The open questions, as well as for the oral part, allow you to evaluate communication skills. For the oral part, see the section of the Biochemistry 2 course. The written exam must always be resumed if the oral exam is not passed.

Glucides: monosacaccharides,disaccharides. Modified sugars. Glycosidic bond. Reserve and structural polysaccharides: glycogen, sulfurized glycosaminoglycans.Lipids. Saturated and unsaturated fatty acids. Nomenclature and structure. Glycerides: triacylglycerols and glycerophospholipids. Sphingolipids: sphingomyelin and glycolipids. Organization of lipids in an aqueous environment: vesicles, micelles, bilayer. Structure of cholesterol and its derivatives: esterified cholesterol, cholic acids, hints on sex hormones and adrenocortical. Organization of cellular and subcellular membranes: general information.
Amino acids: structure, classification based on the side chain. Non-protein amino acids. Amphionic properties of aa. Isoelectric point. Electrophoretic separation of aa; paper and ion exchange column chromatography. Peptide bond: physico-chemical properties. Rotation of bonds around the Cα: impact on the structure. Polypeptides and proteins: separation based on size (gel-filtration) and by affinity. Determination of the molecular mass by SDS-electrophoresis.
Protein structure: primary structure, aa sequence. Secondary structure: alpha helix and beta-sheet. Tertiary structure. Weak stabilization interactions of each structural level. Disulfide bridge bonds. Protein denaturation. Quaternary structure. Methods of studying the structure of proteins: X-ray crystallography and magnetic resonance. Folding errors. APP proteins - beta-amyloid peptides. Glycated proteins.
Structure-function relationship of different protein classes: Immunoglobulins, muscle contractile proteins. Contractile structural unit: morphological and molecular organization. Biochemical mechanism of contraction: role of ATP and calcium ions. Proteins of the intercellular matrix, collagen, laminin and fibronectin. Integrin receptors. Cytoskeleton proteins. Role of integrins in matrix-cell communication. Actin polymerization mechanism and hints on regulatory proteins. Microtubules: structure, polymerization mechanism and intracellular role. Molecular motors: kinesins and dynes. Structure and mechanism of ATP-dependent advancement on the microtubule.
Carrier proteins. Plasma carrier proteins: general information. Process of recognition and bonding. Ka and Kd. Calculation of the degree of saturation. O2-binding proteins. Heme group: structure and interactions with the globin chain. Myoglobin: structure and function. Saturation curve. Hemoglobin: structure. Saturation curve. Allosteria T / R. Interaction between binding sites: cooperativity. Calculation of the degree of cooperativity between equal binding sites belonging to the same oligomeric protein. Hill's coefficient. Regulation of the affinity of Hb for its ligand by: O2, CO2, H + and their role in gas exchange in the lungs and tissues. Role of 2,3 bisphosphoglycerate (BPG) in regulating the affinity of Hb for O2. Maternal-fetal gas exchanges. Molecular basis of hemoglobinopathies: Thalassemia and sickle cell anemia.
Enzymes: general mechanism of action of enzymes. Classification of enzymes. Chemical transformations: thermodynamic aspects. Gibbs free energy. Van’t Hoff equation. Activation energy its impact on the reaction rate.
Speed of reaction. Speed constant. Arrhenius equation. Enzyme kinetics. Hypothesis of steady state. Michaelis-Menten equation. Representation according to Lineweaver-Burk. Fundamental kinetic parameters: meaning and calculation method. PH effect and T effect.
Regulating mechanisms. Activation / inhibition by proteolysis, association / dissociation of subunit. Allosteria: homotropic, heterotropic, positive and negative cooperative effects. Asparticotranscarbamylase. Kinetics of regulatory enzymes: K enzymes and V enzymes. Multiple regulatory mechanisms. Mechanisms of catalysis: induced adaptation, entropic reduction, acid base, covalent. Protease: chymotrypsin, HIV-protease, Thrombin, caspase. Vitamins and cofactors:1) fat-soluble vitamins: structure, bioavailability, mechanism of action of the derived or synthesized cofactors, 2) water-soluble vitamins: structure, bioavailability, mechanism of action of the derived or synthesized cofactors.
Reporting Mechanisms. Generality. Endocrine, paracrine, autocrine mechanisms. Characteristics of the signaling processes: specificity, affinity, cooperativity, amplification, integration. Desensitization and threshold effect. Calculation of the affinity and number of receptors: Scatchard plot.
Classes of receptors.
-Receptors coupled to trimeric G proteins. Downstream effector systems of trimeric G proteins: adenylate cyclase. Mechanism of action of toxins: cholera and pertussis. Beta adrenergic system.
- Voltage dependent and ligand dependent channels. Voltage-dependent neural channel for sodium.
Cholinergic receptor. Phospholipase A-D-C. IP3 and diacylglycerol. Ca-dependent reporting. CaMK. MLCK.
-cADPR and NAADP. PKC. Endocannabinoids: 2-AG. Biochemical mechanisms of sensory perception.
- Tyrosine kinase receptors: structure and signaling mechanism. Route of Ras: MAPK. PI3K Street: AKT / PKB. Src.
- Insulin receptor and downstream signaling pathways. Negative regulation of the TRKs: Cbl. Receptors associated with tyrosine kinase: Jak-Stat. Erythropoietin reporting. Tyrosine phosphatase with receptor-like structure. Serine / threonine kinase receptors. Receptors with cyclase guanylate activity.
-CGMP-dependent reporting. NO synthesis and its role in the cardiovascular system. Inside out and outside signaling mediated by integrins.
Bioenergetics. Basal metabolism. Energy needs in relation to physical activity. Energy consumption by different tissues and organs. Molecules with high energy content: NAD, NADP, FAD, FMN, ATP, phosphocreatine. High energy metabolic intermediates. Esters and thioesters. Role of redox cofactors in catabolic and anabolic processes. Metabolic compartmentalization.
Cellular respiration. Equivalent reducing transport from the cytosol to the mitochondrial matrix: Shuttle systems. Electron transport chain. ATP synthase: structure and rotational mechanism. Mitchell's chemiosmotic theory.
Metabolism: general aspects of catabolism and anabolism. Biochemical aspects of digestion
of food. Role of the pancreas in the digestive process.

In-depth knowledge of human biochemistry and molecular biology; ability to read, understand and comment on a scientific text of cellular biochemistry, also in English; ability to use this knowledge to critically evaluate the objectives and / or results of a research project according to both the quantitative and qualitative approach. Be able to pass the exam in written form with tests to be prepared during the course, and oral.