Unit BIOCHEMISTRY
- Course
- Biotechnology
- Study-unit Code
- 55042606
- Curriculum
- In all curricula
- CFU
- 6
- Course Regulation
- Coorte 2022
- Offered
- 2023/24
- Learning activities
- Caratterizzante
- Area
- Discipline biotecnologiche comuni
- Academic discipline
- BIO/10
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
BIOCHEMISTRY - Canale A
| Code | 55042606 |
|---|---|
| CFU | 6 |
| Teacher | Carla Emiliani |
| Teachers |
|
| Hours |
|
| Learning activities | Caratterizzante |
| Area | Discipline biotecnologiche comuni |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
| Language of instruction | Italian |
| Contents | Aminoacids. Structure and function of proteins. Hemoglobin and myoglobin. Enzymes: enzyme catalysis and kinetics, mechanisms of enzyme control. Molecular constituents and supramolecular architecture of biological membranes. Introduction to the principles of metabolism and bioenergetics. Glycolysis and beta-oxidation of fatty acids. Tricarboxylic acid cycle. Chain electron transport and oxidative phosphorylation. Gluconeogenesis and fatty acid biosynthesis. |
| Reference texts | D. Voet, J.G. Voet, Fondamenti di Biochimica, Ed. Zanichelli Nelson, M.M.Cox, Introduzione alla biochimica di Lehninger, Ed. Zanichelli Nelson, M.M.Cox, Principi di Biochimica |
| Educational objectives | Knowledge: at the end of the course the student will have to know the composition, structural and functional organization of bio-molecules and macromolecules (proteins, lipids, sugars) and their interaction methods. He will also need to know the main metabolic pathways and the molecular mechanisms of the cell's intermediate and energy metabolism. Capacity: at the end of the course the student must be able to relate the knowledge acquired in the abiotic field, in the General Chemistry and Organic Chemistry courses, to a Chemical-Biological field. He must be able to integrate the acquired knowledge into a coherent framework. |
| Prerequisites | In order to be able to understand and profitably attend the Course, it is useful that the student possesses a working knowledge of general and inorganic chemistry, organic chemistry and cell biology. |
| Teaching methods | Lectures on all subjects of the course. Lessons will be integrated with slide projections and movies. |
| Other information | Tutoring activities during the course and the practical training will be performed. For the timetable of lessons please consult the website of the course: http://biotecnologie.unipg.it |
| Learning verification modality | It consists of a written test, followed by an oral one. The written test will serve to ascertain the level of knowledge and ability to understand the topics covered. It will be carried out on It will last a maximum of 40 minutes, during which the student will have to answer thirty multiple choice questions. This will be followed by an oral test to which students who have passed the written test with a grade equal to or higher than 18/30 will have access. This test will serve to clarify critical issues that emerged from the written test and to verify the student's communication skills with language skills and independent organization of the presentation on the topics covered in the written test or in any case covered in class. The outcome of both the written and oral test will contribute to the final grade. Students who have not passed the written test will have the opportunity to analyze the critical issues together with the teacher on the day of the oral test. For information on support services for students with disabilities and/or DSA visit the page http://www.unipg.it/disabilita-e-dsa |
| Extended program | Characteristics and classification of amino acids. Acid-base properties. Modified amino acids and amino acid derivatives. The peptide bond. The isoelectric point of peptides Proteins and their structural levels (primary, secondary, tertiary and quaternary structure). The secondary structure of proteins: alpha-helices, beta sheets, beta folds. Tertiary structure and weak interactions: hydrogen bonds, electrostatic interactions, hydrophobic interactions and van der Waals forces. Protein folding and denaturation. Fibrous proteins: keratin, collagen, fibroin. Myoglobin: structure, heme group, oxygen binding curve. Hemoglobin: oxygen binding curve, T-R state transition. Bohr effect and CO2 transport. Enzymes. Kinetics and reaction coordinates of catalyzed and non-catalyzed reactions. The concept of transition state. Enzyme-substrate interaction. The kinetics of Michaelis and Menten: concept of initial velocity and steady state. The linearization of the Michaelis and Menten equation. Reversible and irreversible inhibitors. Reversible inhibitors: kinetic aspects. Regulation of enzymatic activity: reversible and irreversible mechanisms. Lipids: chemical-physical characteristics. Fatty acids: length, saturation and nomenclature. Triglycerides and phosphoglycerides. Sphingolipids. Cholesterol: characteristics and role in biological membranes. Carbohydrates: aldose and ketose monosaccharides. The epimers. Cycling. Disaccharides: the glycosidic bond. Polysaccharides: reserve and structural functions. Metabolism: endergonic and exergonic reactions. Coupled reactions: the role and structure of ATP. Coenzyme A, pyridine coenzymes, flavin coenzymes. Glycolysis: investment phase and energy recovery phase. Lactic and alcoholic fermentation. Gluconeogenesis: the different stages compared to glycolysis. The pentose phosphate pathway: oxidative phase and non-oxidative phase. Pyruvate dehydrogenase. The Krebs cycle. Anaplerotic reactions. The electron transport chain. The formation of the chemiosmotic gradient. ATP synthase: F0 and F1 subunits. The rotational catalysis of ATP. Beta-oxidation of fatty acids. Ketone bodies. The urea cycle: the synthesis of carbamyl phosphate. The mitochondrial phase and the cytosolic phase. |
BIOCHEMISTRY - Canale B
| Code | 55042606 |
|---|---|
| CFU | 6 |
| Teacher | Lorena Urbanelli |
| Teachers |
|
| Hours |
|
| Learning activities | Caratterizzante |
| Area | Discipline biotecnologiche comuni |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
| Language of instruction | Italian |
| Contents | Aminoacids. Structure and function of proteins. Hemoglobin and myoglobin. Enzymes: enzyme catalysis and kinetics, mechanisms of enzyme control. Molecular constituents and supramolecular architecture of biological membranes. Introduction to the principles of metabolism and bioenergetics. Glycolysis. Tricarboxylic acid cycle. Chain electron transport and oxidative phosphorylation. Gluconeogenesis and pentose-phosphate pathway. Urea cycle. |
| Reference texts | Nelson, M.M.Cox, Introduzione alla biochimica di Lehninger, Ed. Zanichelli - Nelson, M.M.Cox, Principi di Biochimica di Lehninger, Ed. Zanichelli - D. Voet, J.G. Voet, Fondamenti di Biochimica, Ed. Zanichelli |
| Educational objectives | The main purpose of the course is to provide students with a solid knowledge and understanding of biochemistry aimed at understanding the structural and functional properties of biological macromolecules, nutrient metabolism and regulatory mechanisms in biological systems. Main knowledge acquired will be the composition, structural and functional organization of bio-molecules and -macromolecule (proteins, lipids, sugars) and their interaction mechanisms. Students will also gain knowledge of the main metabolic pathways and molecular mechanisms of the cell energetic metabolism. |
| Prerequisites | To attend and profitably understand the Course, it is useful that the student possesses a working knowledge of general chemistry, organic chemistry and cell biology |
| Teaching methods | The course is organized in Lectures on all subjects of the course. Lessons will be integrated with slide projections and movies. |
| Other information | Tutoring activities during the course and the practical training will be performed. For the timetable of lessons please consult the website of the course: http://biotecnologie.unipg.it |
| Learning verification modality | It consists of a preliminary test using the LibreEOL platform with 30 multiple choice questions (4 options, only one correct). Passing the preliminary test allows the final test consisting of three main questions related to the topics covered during the course: one question will be on structural biochemistry, one on metabolism and the third will depend on the general outcome of the exam. This test will aim to verify the student's communication skills with linguistic properties and autonomous organization of the exposure of the topics covered in class; the ability to reason and connect the various topics will also be assessed. |
| Extended program | Characteristics and classification of amino acids. Acid-base properties. Modified amino acids and amino acid derivatives. The peptide bond. Peptide isoelectric point. Protein structural levels (primary, secondary, tertiary and quaternary). Protein secondary structure: alpha-helices, beta sheets, beta folding. Tertiary structure and weak interactions: hydrogen bonds, electrostatic interactions, hydrophobic interactions and van der Waals forces. Protein folding and denaturation. Fibrous proteins: keratin, collagen, fibroin. Myoglobin: structure, heme group, oxygen binding curve. Hemoglobin: oxygen binding curve, T-R state transition. Bohr effect and CO2 transport. The enzymes. Kinetics and reaction coordinate of catalyzed and uncatalyzed reactions. The transition state. Enzyme-substrate interaction. Michaelis and Menten kinetics: concept of initial velocity and steady state. The linearization of the Michaelis-Menten equation. Reversible and irreversible inhibitors. Reversible inhibitors: kinetic aspects. Regulation of enzyme activity: reversible and irreversible mechanisms. Lipids: chemical-physical characteristics. Fatty acids: length, saturation, and nomenclature. Triglycerides and phosphoglycerides. The sphingolipids. Cholesterol: characteristics and role in biological membranes. Carbohydrates: aldose and ketoses monosaccharides. The epimers. The cyclization. Disaccharides: the glycosidic bond. Polysaccharides: reserve and structural functions. Metabolism: endergonic and exergonic reactions. Coupled reactions: the role and structure of ATP. Coenzyme A, pyridine coenzymes, flavin coenzymes. Glycolysis: investment phase and energy recovery phase. Lactic and alcoholic fermentation. Gluconeogenesis: the different stages with respect to glycolysis. The pentose phosphate pathway: oxidative phase and non-oxidative phase. The pyruvate dehydrogenase. The Krebs cycle. Anaplerotic reactions. The electron transport chain. The formation of the chemiosmotic gradient. ATP synthase: F0 and F1 subunits. The rotational catalysis of ATP. The beta-oxidation of fatty acids. Ketone bodies. The urea cycle: the synthesis of carbamyl phosphate. The mitochondrial phase and the cytosolic phase. |
| Obiettivi Agenda 2030 per lo sviluppo sostenibile |