Course program
PART 1: The biological macromolecules
Proteins (8 hours). Water properties. Amino acids and peptide bond. Structure and function of proteins. Structural levels. Fibrous and globular proteins. Protein folding and denaturation. Dynamic properties of proteins.
Myoglobin and hemoglobin (6 hours). Physiological role. Tertiary and quaternary structure. Cooperation of the link with oxygen. Concerted and sequential allosteric models. Bohr effect and allosteric effectors. Pathological hemoglobins and molecular diseases.
Enzymology (8 hours). General characteristics of enzymes. General theory of enzymatic catalysis. Enzymatic kinetics. Reversible inhibition mechanisms. Mechanisms of enzymatic catalysis. Role of vitamins and coenzymes in catalysis. Regulation of enzymatic activity.
Lipids (4 hours). Structure and function. Biological membranes. Fat-soluble vitamins.
Glucidi (2 hours). Structure and function. Disaccharides and polysaccharides. Glycoproteins.
Nucleic acids (2 hours). Structure of purine and pyrimidine bases, nucleosides and nucleotides.
PART 2: Biochemical methodologies
Biochemical methods and techniques (8 hours). Protein purification strategies. Dosage of proteins. Chromatographic and electrophoretic techniques. Mass spectrometry. Dosage of enzymes. Techniques for determining the primary structure and the three-dimensional structure of proteins.
PART 3: Metabolism
General aspects of metabolism (4 hours). Fundamental principles of thermodynamics applied to biological systems. Role of ATP and high-energy compounds in energy metabolism. Electron transporters. Redox reactions. Mechanisms of metabolic regulation.
Metabolic pathways and their regulation (18 hours). Glycolysis, alcoholic and homolactic fermentation. Via of the pentose phosphate. Gluconeogenesis. Cori cycle. Glycogen metabolism. Pyruvate dehydrogenase. Cycle of tricarboxylic acids. Glyoxylate cycle. Degradation and synthesis of fatty acids. Chetonic bodies. Cholesterol synthesis. Metabolism of protein nitrogen and degradation of amino acids. Glucose-alanine cycle. Urea cycle. Transporters of monocarbon units. Electron transport chain. Oxidative phosphorylation. Malate-aspartate and glycerophosphate shuttle systems.
Hormonal regulation and signal transduction (2 hours).
Prerequisites
1) ESSENTIAL. Knowledge of the basic concepts of general chemistry and organic chemistry. In particular, it is necessary to know: a) the properties of the main functional groups; b) the mechanism of nucleophilic substitution and addition reactions; c) the concept of acid, base and pH; d) the properties of the buffer solutions.
2) IMPORTANT. Principles and laws of thermodynamics; concept of chemical equilibrium; fundamentals of chemical kinetics.
Books
• David L Nelson, Michael M Cox, I principi di biochimica di Lehninger, Zanichelli.
• Donald Voet, Judith G Voet, Charlotte W Pratt, Fondamenti di biochimica, Zanichelli
• Garrett - Grisham, Biochimica, Piccin
• Appling, Anthony-Cahill, Mathews, Biochimica. Molecole e Metabolismo, PEARSON
• All teaching materials filed at the site: elearning2.uniroma1.it
Teaching mode
The course will be carried out through theoretical lectures (64 hours), theoretical exercises in the classroom (6 hours) and practical laboratory experiences (6 hours).
The anticovid rules have changed the teaching method that takes place in a mixed mode: in presence and at a distance.
The modalities with which the laboratory activities will take place will be established on the basis of Sapienza's anticovid regulations in force
Frontal lessons:
1) Explanation of the topics covered by the program through slide projection and audiovisual material. This didactic model is aimed at providing the theoretical knowledge of Biochemistry.
2) Open discussions of the lesson topics, during which students are called to intervene, which aim to develop communication, criticism and judgment skills.
Theoretical exercises in the classroom:
1) Screening and discussion of videos on protein purification (2 hours in class)
2) Projection and discussion of videos on electrophoresis (2 hours in class)
3) Practical exercise on the use of molecular models (2 hours in class)
The exercises aim to deepen the theoretical concepts studied in class and put them into practice.
Laboratory experiences:
1) Computer simulation of protein purification (2 hours in the computer lab)
2) Chromatographic separation of proteins and small molecules (2 hours of practical activity in the laboratory).
3) Measurements of enzymatic kinetics (2 hours of practical activity in the laboratory).
The laboratory experiences aim to put into practice the theoretical concepts studied in class, develop the ability to plan an experiment and interpret it, increase critical and judgment skills.
Frequency
Attendance is optional but strongly recommended
Exam mode
Students will be able to take two ongoing written tests (exemptions) in order to facilitate passing the exam in the months between June and September. The exemption will focus on these topics (with reference to the detailed program available on the Elearning page of the course: https : //elearning.uniroma1.it/course/view.php? id = 1513):
water
amino acids
structure and function of proteins,
biochemical methodologies
myoglobin and hemoglobin
lipids, membranes, carbohydrates
enzymology
Once the exemption has been passed, the oral exam will focus on the remaining part of the program (please note that it cannot be excluded that during the interview it is necessary to recall concepts developed in the first part of the program):
general aspects of metabolism
metabolic pathways and their regulation
The overall mark will be given by the arithmetic average of the mark of the exemptions and of the oral exam.
The student who for whatever reason is not in possession of a valid exemption, will take the oral exam on the whole program.
Reference site: https://elearning.uniroma1.it/course/view.php?id=1513
Bibliography
Hageman, James H. "Use of molecular models for active learning in biochemistry lecture courses." Journal of Chemical Education 87.3 (2010): 291-293.
Abreu, Paula Alvarez, et al. "Computational strategy for visualizing structures and teaching biochemistry." Biochemistry and Molecular Biology Education 47.1 (2019): 76-84.
Bottomley, Steven, and Paul Denny. "A participatory learning approach to biochemistry using student authored and evaluated multiple‐choice questions." Biochemistry and Molecular Biology Education 39.5 (2011): 352-361.
White, Harold B., et al. "What skills should students of undergraduate biochemistry and molecular biology programs have upon graduation?." Biochemistry and molecular biology education 41.5 (2013): 297-301.
Lesson mode
The course will be carried out through theoretical lectures (64 hours), theoretical exercises in the classroom (6 hours) and practical laboratory experiences (6 hours).
The anticovid rules have changed the teaching method that takes place in a mixed mode: in presence and at a distance.
The modalities with which the laboratory activities will take place will be established on the basis of Sapienza's anticovid regulations in force
Frontal lessons:
1) Explanation of the topics covered by the program through slide projection and audiovisual material. This didactic model is aimed at providing the theoretical knowledge of Biochemistry.
2) Open discussions of the lesson topics, during which students are called to intervene, which aim to develop communication, criticism and judgment skills.
Theoretical exercises in the classroom:
1) Screening and discussion of videos on protein purification (2 hours in class)
2) Projection and discussion of videos on electrophoresis (2 hours in class)
3) Practical exercise on the use of molecular models (2 hours in class)
The exercises aim to deepen the theoretical concepts studied in class and put them into practice.
Laboratory experiences:
1) Computer simulation of protein purification (2 hours in the computer lab)
2) Chromatographic separation of proteins and small molecules (2 hours of practical activity in the laboratory).
3) Measurements of enzymatic kinetics (2 hours of practical activity in the laboratory).
The laboratory experiences aim to put into practice the theoretical concepts studied in class, develop the ability to plan an experiment and interpret it, increase critical and judgment skills.