Select Academic Year:     2016/2017 2017/2018 2018/2019 2019/2020 2020/2021 2021/2022
Professor
TIZIANA CABRAS (Tit.)
Period
Annual 
Teaching style
Convenzionale 
Lingua Insegnamento
 



Informazioni aggiuntive

Course Curriculum CFU Length(h)
[70/88]  CHEMICAL AND BIOTECHNOLOGICAL PROCESS ENGINEERING [88/00 - Ord. 2020]  PERCORSO COMUNE 6 60

Objectives

1. Knowledge and understanding:
The aim of the course is the understanding of the molecular basis of biological systems, and of the biochemical mechanisms that regulate the cellular metabolic activities by the knowledge of:
- structure, properties, function, interactions and metabolic reactions of the bio-molecules (proteins, carbohydrates, lipids, nucleic acids);
- functionality and regulation of the enzymes;
- production and maintenance of the energy.
In addition, knowledge of the main specific metabolic pathways of organs and tissues that are the basis of their correct functionality in humans (liver, nervous system, muscle and adipose tissue, endocrine system, blood, kidney), in order to reach an understanding of the metabolic interrelationships between the various tissues in different physiological conditions, and the understanding of the biochemical basis of some metabolic pathologies.


2. Applying knowledge and understanding:
To write structures of the main classes of biomolecules; to interpret the titration curves of amino acids and deduce acid/base properties of peptides/proteins; to interpret and elaborate binding curves, such as that of the respiratory proteins, and enzymatic kinetic (Micaelis/Menten; allosteric enzymes); to apply knowledge and understanding of structures, chemical bonds and properties of the biomolecules to study metabolic reaction mechanisms; to elaborate and integrate the metabolic pathways that occur in specific organs and tissues, of their regulation and integration and of the interrelationships existing between the different organs and tissues in different physio-pathological conditions.

3. Making judgements: learning the fundamental concepts of Biochemistry will consolidate the student scientific culture and therefore it will allow the autonomous making judgements for the interpretation of the experimental data and in the deepening of their knowledge both in their work area and outside it. Application of the acquired knowledges develops in the students discreet critical skills in molecular issues and the development of interesting analytical capabilities for the results that can be applied in various professional.

4. Communication skills: Acquisition of the ability to expose and explain in a simple but rigorous manner and with the appropriate technical language the molecular processes underlying the living systems.

5. Learning skills: Acquisition of the learning ability necessary to connect and integrate the knowledge learned from those provided in the previous and subsequent courses, and, moreover, to utilize different bibliographic sources to upload continuously their knowledge, and that necessary to start successive and high-level studies (doctorate, specialization schools).

Prerequisites

To attend the lessons is essential to have acquired the knowledge of General and Inorganic Chemistry, and of cellular Biology. The knowledge of Analitical Chemistry and Organic Chemistry are fundamental.
Prerequisites Corsi di Laurea V.O. (D.M. 509/99): Animal Biology - Organic Chemistry - Analytical Chemistry.
Prerequisites Corsi di Laurea N.O. (D.M. 270/04): Animal Biology - Organic Chemistry (only frequency) - Analytical Chemistry.

Contents

• Amino acids. Structure and stereochemistry. Classification. Acid-base properties of amino acids: Titration curve, pKa, isoelectric point.
• Peptides and Proteins. Characteristics and properties of the peptide bond. Ionization of the peptides/proteins. Structural organization of the proteins. Secondary structures. Fibrous proteins, collagen. Tertiary structure and globular proteins. Polymeric proteins. Post-translational modifications. Immunoglobulins. Glycated proteins.
• Hemoproteins. The heme moiety. Myoglobin and hemoglobin oxygen binding curve. Allosteric properties of the hemoglobin, modulators of the oxygen binding. Physiological variants of Hb. Cytoglobin and Neuroglobin
• Carbohydrates. Nomenclature. Stereochemistry. The anomeric forms and Haworth projections. Derivatives of the sugars. The glycosidic bond. Disaccharides of biological significance. The polysaccharides. Structure of amylose, amylopectin, glycogen and cellulose.
• Nucleotides and nucleic acids. The purine and pyrimidine bases. The nucleotides. Structure and biological role of DNA, and RNA.
• Lipids. Fatty acids. Classification, glycerophospholipids, sphingolipids, cholesterol. Structure and functions. Biological membranes.
• Enzymes. Classification and properties of the enzymes. The kinetic of the enzymes. Effects of pH and temperature. Significance of Km, Vmax and Kcat. Action of irreversible and reversible inhibitors. The Micaelis-Menten equation and the interpretation of the graphics. Double reciprocal plot. Mechanisms of enzyme catalysis, examples. Regulation of the enzyme activity in vivo.
• Vitamins. Liposoluble and hydrosoluble vitamins, structure and biological role. Coenzymes and their reaction mechanism. Vitamin-like factors.
• Bioenergetics. G, G0 and Keq. Compounds with high hydrolysis energy, phosphorylation at the substrate level and ATP cycle.
• Oxidative phosphorylation. The respiratory mitochondrial chain, its components and their organization. The chemiosmosis theory. ATP synthesis.
• Glucidic metabolism. Glycolysis and its regulation. Fermentations. Shuttle systems of the cytosolic NADH. Pyruvate metabolism. Metabolism of other monosaccharides. Gluconeogenesis. Biosynthesis and degradation of glycogen. Hormonal control of the glucidic metabolism. The pentose-phosphates cycle.
• Krebs cycle. Chemical reactions and their metabolic regulation.
• Metabolism of the lipids. Plasmatic lipoproteins. Mobilization of fatty acids. -oxidation, hormonal and metabolic regulation. Ketogenesis. Biosynthesis of the fatty acids. Synthesis of triglycerides. Metabolism of glycerophospholipids. Cholesterol metabolism.
• Metabolism of the amino acids. Protein digestion. Protein turnover. Metabolic role of amino acids. Transamination, deamination, decarboxylation. Biogenic amines. NO-synthase. Formation and transport of ammonia, ureogenesis.
• EME metabolism. Iron metabolism. Heme biosynthesis and catabolism..
• Hormone metabolism. Receptors. Mechanisms of action. Pancreatic hormones. Thyroid hormones. Pituitary hormones. Adrenal hormones. Corticosteroids. Eicosanoids.
• Hepatic metabolic processes. Coordination of the metabolisms. Detoxification processes. Metabolism of ethanol.
• Biochemistry of muscle tissue. Mechanism of muscle contraction. Aerobic and anaerobic processes.
• Biochemistry of adipose tissue. Metabolism and secretory function. Thermogenesis.
• Metabolic correlations. Fasting-nutrition cycle. Metabolic correlations in different nutritional and hormonal states.
• Biochemistry of cancer cells. Warburg effect. Krebs cycle and Glutamine. Metabolic regulation of oncogenes and tumor suppressors.

Teaching Methods

The course begins in November (6 hours of weekly lesson), overal 96 hours of frontal lessons: 30 hours on the structure of biomolecules and their biological properties (sugars, lipids, nucleic acids, amino acids and proteins, hemoproteins); 16 hours on the enzyme and on the structure and function of the coenzymes; 50 on bioenergetics and metabolism.

Tutorial activities will take place outside the lesson time and consist of exercises and insights to help the student learn the biomolecular structures, acid-base properties of amino acids and peptides, interpretation of oxygen / hemoglobin binding curves, enzymatic kinetics.
Teacher will provide individual explanations during the reception schedule by appointment.
To assist with the study, the teacher will provide lecture slides, and provides exercise books and copies of previous written tests.
To meet specific educational needs related to the Covid-19 epidemiological situation, the possibility of live streaming lessons or recordings of the same available online is provided. In addition, the teaching will be delivered simultaneously both in presence and online, in order to be enjoyed in university classrooms but at the same time also remotely.

Verification of learning

Written and oral examination. The written tests in itinere assessable for the examination may be carried out in the 2nd half of the year provided that the safety protocols and the contextual conditions linked to the Covid-19 pandemic allow teaching to be carried out entirely in the presence. If the conditions do not occur, Biochemistry will be fully verified by the oral exam.
For attending students, the following written tests will be carried out during the course:
-Structure and acid-base properties of amino acids and peptides; Structure of proteins, sugars, lipids, nucleotides and ac. nucleic; Biological membranes. Respiratory protein properties. Interpretation of binding curves.
-Environmental kinetics, interpretation of graphs; Catalysis and regulation mechanisms.
The ratings of the verifications are considered for the final evaluation. The exam is scored out of a maximum of 30 points. Questions to which the student responds insufficiently or incorrectly will be verified in the oral examination.
The student may repeat, on the day of the exam, the written tests he believes he can improve. For non-attending students, on the day of examination, a single written assignment in order to access to oral examination.
The total score, in thirtieths is the result of the weighted average of written tests and oral exam.
• 30 cum laude: excellent knowledge of all subjects, accurate, detailed and enriched critical and personal points of view, ability to describe an overview of metabolic processes, excellent communicative ability, broad judgment autonomy, and learning abilities.
• 30: Acquire all the required knowledge, ability to apply them to the resolution of analytic problems proposed in the exams. Precise and impeccable oral exposure to language skills and communicative skills, judgmental autonomy and excellent learning skills.
• 27-29: Acquisition of all required knowledge, ability to solve analytic problems. Exposure to the correct but not detailed or inaccurate arguments. Autonomy of judgment, communication skills and good and appropriate learning skills.
• 25-26: Acquiring the knowledge required and ability to use them in the processing of biochemical topics, albeit with slight gaps, fluid but imprecise exposure. Autonomy of judgment, communicative abilities and discrete learning abilities.
• 22-24: poor acquisition of required knowledge, skills in imprecise and incomplete arguments. Errors in writing structure and ties. Adequate communication skills, autonomy of judgment and appropriate learning skills, even with some uncertainty.
• 18-21: acquiring the minimum knowledge on the topics studied, allowing them to write the structure of the most important biomolecules and to argue the basics of enzymatic kinetics, metabolism, and the main techniques of purification and characterization of proteins. Difficulties in solving the proposed analytic problems. Poor language skills and communication skills, skills, judgment autonomy, and just as much learning ability as a whole.

Texts

• Amino acids. Structure and stereochemistry. Classification. Acid-base properties of amino acids: Titration curve, pKa, isoelectric point.
• Peptides and Proteins. Characteristics and properties of the peptide bond. Ionization of the peptides/proteins. Structural organization of the proteins. Secondary structures. Fibrous proteins, collagen. Tertiary structure and globular proteins. Polymeric proteins. Post-translational modifications. Immunoglobulins. Glycated proteins.
• Hemoproteins. The heme moiety. Myoglobin and hemoglobin oxygen binding curve. Allosteric properties of the hemoglobin, modulators of the oxygen binding. Physiological variants of Hb. Cytoglobin and Neuroglobin
• Carbohydrates. Nomenclature. Stereochemistry. The anomeric forms and Haworth projections. Derivatives of the sugars. The glycosidic bond. Disaccharides of biological significance. The polysaccharides. Structure of amylose, amylopectin, glycogen and cellulose.
• Nucleotides and nucleic acids. The purine and pyrimidine bases. The nucleotides. Structure and biological role of DNA, and RNA.
• Lipids. Fatty acids. Classification, glycerophospholipids, sphingolipids, cholesterol. Structure and functions. Biological membranes.
• Enzymes. Classification and properties of the enzymes. The kinetic of the enzymes. Effects of pH and temperature. Significance of Km, Vmax and Kcat. Action of irreversible and reversible inhibitors. The Micaelis-Menten equation and the interpretation of the graphics. Double reciprocal plot. Mechanisms of enzyme catalysis, examples. Regulation of the enzyme activity in vivo.
• Vitamins. Liposoluble and hydrosoluble vitamins, structure and biological role. Coenzymes and their reaction mechanism. Vitamin-like factors.
• Bioenergetics. G, G0 and Keq. Compounds with high hydrolysis energy, phosphorylation at the substrate level and ATP cycle.
• Oxidative phosphorylation. The respiratory mitochondrial chain, its components and their organization. The chemiosmosis theory. ATP synthesis.
• Glucidic metabolism. Glycolysis and its regulation. Fermentations. Shuttle systems of the cytosolic NADH. Pyruvate metabolism. Metabolism of other monosaccharides. Gluconeogenesis. Biosynthesis and degradation of glycogen. Hormonal control of the glucidic metabolism. The pentose-phosphates cycle.
• Krebs cycle. Chemical reactions and their metabolic regulation.
• Metabolism of the lipids. Plasmatic lipoproteins. Mobilization of fatty acids. -oxidation, hormonal and metabolic regulation. Ketogenesis. Biosynthesis of the fatty acids. Synthesis of triglycerides. Metabolism of glycerophospholipids. Cholesterol metabolism.
• Metabolism of the amino acids. Protein digestion. Protein turnover. Metabolic role of amino acids. Transamination, deamination, decarboxylation. Biogenic amines. NO-synthase. Formation and transport of ammonia, ureogenesis.
• EME metabolism. Iron metabolism. Heme biosynthesis and catabolism..
• Hormone metabolism. Receptors. Mechanisms of action. Pancreatic hormones. Thyroid hormones. Pituitary hormones. Adrenal hormones. Corticosteroids. Eicosanoids.
• Hepatic metabolic processes. Coordination of the metabolisms. Detoxification processes. Metabolism of ethanol.
• Biochemistry of muscle tissue. Mechanism of muscle contraction. Aerobic and anaerobic processes.
• Biochemistry of adipose tissue. Metabolism and secretory function. Thermogenesis.
• Metabolic correlations. Fasting-nutrition cycle. Metabolic correlations in different nutritional and hormonal states.
• Biochemistry of cancer cells. Warburg effect. Krebs cycle and Glutamine. Metabolic regulation of oncogenes and tumor suppressors.

More Information

Teacher will provide individual explanations during the reception schedule by appointment.
To assist with the study, the teacher will provide lecture slides, and provides exercise books and copies of previous written tests.

Questionnaire and social

Share on: