Unit BIOCHEMISTRY II
- Course
- Medicine and surgery
- Study-unit Code
- 50202109
- Curriculum
- In all curricula
- CFU
- 13
- Course Regulation
- Coorte 2025
- Offered
- 2025/26
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa integrata
BIOCHEMISTRY OF HORMONES AND TISSUES
| Code | A004713 |
|---|---|
| CFU | 3 |
| Teacher | Barbara Cellini |
| Teachers |
|
| Hours |
|
| Learning activities | Base |
| Area | B_02. struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Sector | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
METABOLIC BIOCHEMISTRY I
| Code | A004711 |
|---|---|
| CFU | 3 |
| Teacher | Barbara Cellini |
| Teachers |
|
| Hours |
|
| Learning activities | Base |
| Area | B_02. struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Sector | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
METABOLIC BIOCHEMISTRY II
| Code | A004712 |
|---|---|
| CFU | 3 |
| Teacher | Barbara Cellini |
| Teachers |
|
| Hours |
|
| Learning activities | Base |
| Area | B_02. struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Sector | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
BIOCHEMISTRY 1
| Code | A005634 |
|---|---|
| CFU | 2 |
| Learning activities | Base |
| Area | B_02. struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Sector | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 2
- Teacher
- Ilaria Bellezza
- Teachers
- Ilaria Bellezza
- Hours
- 25 ore - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Functional biochemistry
- Reference texts
- Biochimica Medica – Siliprandi, Tettamanti - Piccin editore
I principi di biochimica di Lehninger-Nelson, Cox – Zanichelli Editore
Fondamenti di biochimica umana- Maccarrone- Zanichelli Editore - Educational objectives
- The course aims to provide students with in-depth knowledge of:
– protein structure and function;
– vitamins and coenzymes;
– biological membranes;
– principles of bioenergetics.
Upon completion of the course, students will be able to critically describe the structure–function relationships of proteins and the molecular mechanisms underlying enzymatic catalysis, as well as the processes of transport across biological membranes and the main mechanisms of biosignaling. In addition, students will acquire the ability to interpret metabolic processes in accordance with the principles of thermodynamics, with particular emphasis on the mechanisms of chemical energy conservation and transformation. - Prerequisites
- To successfully follow the Biochemistry course, it is necessary to have acquired basic knowledge of Chemistry and introductory Biochemistry, as well as Biology, as outlined in the syllabus of the semester filtro.
- Teaching methods
- The course is organized as follows:
Lectures covering all topics of the syllabus. During the lectures, students are encouraged to participate and ask for clarification.
Scheduled meetings, held in the classroom or via the Teams platform, for clarification and in-depth discussion.
Exercises and test simulations carried out using interactive teaching methodologies, such as the Wooclap application or Microsoft Forms. - Other information
- Teaching activities will take place according to the schedule published on the website of the Degree Program in Medicine and Surgery.
Location: Department of Medicine and Surgery.
For information on dispensatory measures that can be implemented for students with DSA and/or disabilities, see the page: http://www.unipg.it/disabilita-e-dsa - Learning verification modality
- The exam consists of a written test comprising 52 multiple-choice questions covering all topics of the syllabus. The test will be graded by awarding 0.6 points for each correct answer, 0 points for each unanswered question, and applying a penalty of -0.15 points for each incorrect answer.
The written test will assess detailed knowledge of the functional properties of macromolecules and metabolic reactions, including the chemical structures of the compounds involved, the mechanisms regulating these reactions, and the integration of metabolism among the different tissues of the organism.
After passing the written test, students are given the opportunity to take an oral examination covering all course topics. The oral exam aims to evaluate the level of subject knowledge as well as the ability to make connections and integrate knowledge, also in relation to the future medical profession. The oral exam will also assess the student’s communication skills and appropriate use of scientific terminology. - Extended program
- PROTEIN STRUCTURE AND FUNCTION. Review of amino acids and proteins. Fibrous proteins: collagen (structure, function, post-translational modifications, collagen-related pathologies, role of vitamin C); a-keratin (structure and function); myosin (structure and function). Protein folding: thermodynamics and kinetics, protein aggregation, heat shock proteins (HSP 60, 70, 90), protein disulfide isomerase, peptidyl-prolyl isomerase.
Hemoglobin and myoglobin: heme group (basic structural features, interaction with the polypeptide chain, function), myoglobin structure and oxygen-binding curve; hemoglobin structure, conformational states, oxygen saturation curve, allosteric modulators (O2, CO2, H¿, 2,3-BPG), CO2 transport, hemoglobin variants (HbF, HbS, methemoglobins, glycated hemoglobin).
Enzymes: general properties, classification, active site, thermodynamics of catalyzed reactions, activation energy, binding energy, induced fit, factors affecting reaction rate (pH, temperature, substrate concentration), enzyme kinetics (Michaelis–Menten kinetics), kinetic parameters, multi-substrate reactions, enzyme inhibition (irreversible inhibitors, competitive, uncompetitive, and mixed inhibitors). Catalytic mechanisms: acid–base catalysis, metal ion catalysis, covalent catalysis; serine proteases (catalytic mechanism, induced fit, stabilization of intermediates, substrate specificity). Allosteric modulators. Reversible covalent modifications (e.g., phosphorylation), irreversible covalent modifications (e.g., limited proteolysis). Regulation of protein half-life (e.g., ubiquitin–proteasome system).
VITAMINS AND COENZYMES. Ascorbic acid, thiamine, lipoic acid, riboflavin, niacin, pantothenic acid, pyridoxine, biotin, folic acid, vitamin B12. Overview of the functions of fat-soluble vitamins (A, K, D, E). Pyruvate dehydrogenase complex (structure and catalytic mechanism). - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- 3: Health and well-being.
4: Quality education
Cognomi M-Z
- CFU
- 2
- Teacher
- Ilaria Bellezza
- Teachers
- Ilaria Bellezza
- Hours
- 25 ore - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Functional biochemistry
- Reference texts
- Biochimica Medica – Siliprandi, Tettamanti - Piccin editore
I principi di biochimica di Lehninger-Nelson, Cox – Zanichelli Editore
Fondamenti di biochimica umana- Maccarrone- Zanichelli Editore - Educational objectives
- The course aims to provide students with in-depth knowledge of:
– protein structure and function;
– vitamins and coenzymes;
– biological membranes;
– principles of bioenergetics.
Upon completion of the course, students will be able to critically describe the structure–function relationships of proteins and the molecular mechanisms underlying enzymatic catalysis, as well as the processes of transport across biological membranes and the main mechanisms of biosignaling. In addition, students will acquire the ability to interpret metabolic processes in accordance with the principles of thermodynamics, with particular emphasis on the mechanisms of chemical energy conservation and transformation. - Prerequisites
- To successfully follow the Biochemistry course, it is necessary to have acquired basic knowledge of Chemistry and introductory Biochemistry, as well as Biology, as outlined in the syllabus of the semester filtro.
- Teaching methods
- The course is organized as follows:
Lectures covering all topics of the syllabus. During the lectures, students are encouraged to participate and ask for clarification.
Scheduled meetings, held in the classroom or via the Teams platform, for clarification and in-depth discussion.
Exercises and test simulations carried out using interactive teaching methodologies, such as the Wooclap application or Microsoft Forms. - Other information
- Teaching activities will take place according to the schedule published on the website of the Degree Program in Medicine and Surgery.
Location: Department of Medicine and Surgery.
For information on dispensatory measures that can be implemented for students with DSA and/or disabilities, see the page: http://www.unipg.it/disabilita-e-dsa - Learning verification modality
- The exam consists of a written test comprising 52 multiple-choice questions covering all topics of the syllabus. The test will be graded by awarding 0.6 points for each correct answer, 0 points for each unanswered question, and applying a penalty of -0.15 points for each incorrect answer.
The written test will assess detailed knowledge of the functional properties of macromolecules and metabolic reactions, including the chemical structures of the compounds involved, the mechanisms regulating these reactions, and the integration of metabolism among the different tissues of the organism.
After passing the written test, students are given the opportunity to take an oral examination covering all course topics. The oral exam aims to evaluate the level of subject knowledge as well as the ability to make connections and integrate knowledge, also in relation to the future medical profession. The oral exam will also assess the student’s communication skills and appropriate use of scientific terminology. - Extended program
- PROTEIN STRUCTURE AND FUNCTION. Review of amino acids and proteins. Fibrous proteins: collagen (structure, function, post-translational modifications, collagen-related pathologies, role of vitamin C); a-keratin (structure and function); myosin (structure and function). Protein folding: thermodynamics and kinetics, protein aggregation, heat shock proteins (HSP 60, 70, 90), protein disulfide isomerase, peptidyl-prolyl isomerase.
Hemoglobin and myoglobin: heme group (basic structural features, interaction with the polypeptide chain, function), myoglobin structure and oxygen-binding curve; hemoglobin structure, conformational states, oxygen saturation curve, allosteric modulators (O2, CO2, H¿, 2,3-BPG), CO2 transport, hemoglobin variants (HbF, HbS, methemoglobins, glycated hemoglobin).
Enzymes: general properties, classification, active site, thermodynamics of catalyzed reactions, activation energy, binding energy, induced fit, factors affecting reaction rate (pH, temperature, substrate concentration), enzyme kinetics (Michaelis–Menten kinetics), kinetic parameters, multi-substrate reactions, enzyme inhibition (irreversible inhibitors, competitive, uncompetitive, and mixed inhibitors). Catalytic mechanisms: acid–base catalysis, metal ion catalysis, covalent catalysis; serine proteases (catalytic mechanism, induced fit, stabilization of intermediates, substrate specificity). Allosteric modulators. Reversible covalent modifications (e.g., phosphorylation), irreversible covalent modifications (e.g., limited proteolysis). Regulation of protein half-life (e.g., ubiquitin–proteasome system).
VITAMINS AND COENZYMES. Ascorbic acid, thiamine, lipoic acid, riboflavin, niacin, pantothenic acid, pyridoxine, biotin, folic acid, vitamin B12. Overview of the functions of fat-soluble vitamins (A, K, D, E). Pyruvate dehydrogenase complex (structure and catalytic mechanism). - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- 3: Health and well-being.
4: Quality education
BIOCHEMISTRY 2
| Code | A005635 |
|---|---|
| CFU | 2 |
| Learning activities | Base |
| Area | B_02. struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Sector | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 2
- Teacher
- Davide Chiasserini
- Teachers
- Ilaria Bellezza (Codocenza)
- Hours
- 25 ore (Codocenza) - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Functional biochemistry
- Reference texts
- Biochimica Medica – Siliprandi, Tettamanti - Piccin editore
I principi di biochimica di Lehninger-Nelson, Cox – Zanichelli Editore
Fondamenti di biochimica umana- Maccarrone- Zanichelli Editore - Educational objectives
- The course aims to provide students with in-depth knowledge of:
– protein structure and function;
– vitamins and coenzymes;
– biological membranes;
– principles of bioenergetics.
Upon completion of the course, students will be able to critically describe the structure–function relationships of proteins and the molecular mechanisms underlying enzymatic catalysis, as well as the processes of transport across biological membranes and the main mechanisms of biosignaling. In addition, students will acquire the ability to interpret metabolic processes in accordance with the principles of thermodynamics, with particular emphasis on the mechanisms of chemical energy conservation and transformation. - Prerequisites
- To successfully follow the Biochemistry course, it is necessary to have acquired basic knowledge of Chemistry and introductory Biochemistry, as well as Biology, as outlined in the syllabus of the semester filtro.
- Teaching methods
- The course is organized as follows:
Lectures covering all topics of the syllabus. During the lectures, students are encouraged to participate and ask for clarification.
Scheduled meetings, held in the classroom or via the Teams platform, for clarification and in-depth discussion.
Exercises and test simulations carried out using interactive teaching methodologies, such as the Wooclap application or Microsoft Forms. - Other information
- Teaching activities will take place according to the schedule published on the website of the Degree Program in Medicine and Surgery.
Location: Department of Medicine and Surgery.
For information on dispensatory measures that can be implemented for students with DSA and/or disabilities, see the page: http://www.unipg.it/disabilita-e-dsa - Learning verification modality
- The exam consists of a written test comprising 52 multiple-choice questions covering all topics of the syllabus. The test will be graded by awarding 0.6 points for each correct answer, 0 points for each unanswered question, and applying a penalty of -0.15 points for each incorrect answer.
The written test will assess detailed knowledge of the functional properties of macromolecules and metabolic reactions, including the chemical structures of the compounds involved, the mechanisms regulating these reactions, and the integration of metabolism among the different tissues of the organism.
After passing the written test, students are given the opportunity to take an oral examination covering all course topics. The oral exam aims to evaluate the level of subject knowledge as well as the ability to make connections and integrate knowledge, also in relation to the future medical profession. The oral exam will also assess the student’s communication skills and appropriate use of scientific terminology. - Extended program
- BIOLOGICAL MEMBRANES. Review of lipids and biological membranes. Membrane transport: transmembrane proteins (structural properties), thermodynamics of transport, simple diffusion, facilitated transport (GLUT transporters, chloride–bicarbonate exchanger, K¿ channels, aquaporins), primary active transport (Na¿/K¿ pump, SERCA pump, ABC transporters), secondary active transport. Biosignaling: general features; GPCRs (Gs, Gi, Gq; signal transduction and termination), receptor tyrosine kinases (mechanism of action and signal termination), cyclic GMP, nitric oxide (NO), second messengers derived from phosphatidylcholine and sphingomyelin, steroid hormone receptors (mechanism of action).
BIOENERGETICS. Review of ATP structure. Introduction to metabolism: general features of metabolism (catabolism and anabolism), thermodynamics of metabolic processes, energetic role of ATP and its additional functions. Substrate-level phosphorylation: 1,3-bisphosphoglycerate, phosphocreatine, phosphoenolpyruvate, succinyl-CoA, thermodynamic aspects. Oxidative phosphorylation: redox reactions, oxidation states of carbon, electron transport chain (structure and function of respiratory chain complexes), reactive oxygen species, oxidative stress and antioxidant defenses (GSH), chemiosmotic coupling, ATP synthase (structure and mechanism of rotational catalysis), thermodynamic and quantitative aspects, regulation of oxidative phosphorylation, inhibitors and uncoupling agents. - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- 3: Health and well-being.
4: Quality education
Cognomi M-Z
- CFU
- 2
- Teacher
- Davide Chiasserini
- Teachers
- Ilaria Bellezza (Codocenza)
- Hours
- 25 ore (Codocenza) - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Functional biochemistry
- Reference texts
- Biochimica Medica – Siliprandi, Tettamanti - Piccin editore
I principi di biochimica di Lehninger-Nelson, Cox – Zanichelli Editore
Fondamenti di biochimica umana- Maccarrone- Zanichelli Editore - Educational objectives
- The course aims to provide students with in-depth knowledge of:
– protein structure and function;
– vitamins and coenzymes;
– biological membranes;
– principles of bioenergetics.
Upon completion of the course, students will be able to critically describe the structure–function relationships of proteins and the molecular mechanisms underlying enzymatic catalysis, as well as the processes of transport across biological membranes and the main mechanisms of biosignaling. In addition, students will acquire the ability to interpret metabolic processes in accordance with the principles of thermodynamics, with particular emphasis on the mechanisms of chemical energy conservation and transformation. - Prerequisites
- To successfully follow the Biochemistry course, it is necessary to have acquired basic knowledge of Chemistry and introductory Biochemistry, as well as Biology, as outlined in the syllabus of the semester filtro.
- Teaching methods
- The course is organized as follows:
Lectures covering all topics of the syllabus. During the lectures, students are encouraged to participate and ask for clarification.
Scheduled meetings, held in the classroom or via the Teams platform, for clarification and in-depth discussion.
Exercises and test simulations carried out using interactive teaching methodologies, such as the Wooclap application or Microsoft Forms. - Other information
- Teaching activities will take place according to the schedule published on the website of the Degree Program in Medicine and Surgery.
Location: Department of Medicine and Surgery.
For information on dispensatory measures that can be implemented for students with DSA and/or disabilities, see the page: http://www.unipg.it/disabilita-e-dsa - Learning verification modality
- The exam consists of a written test comprising 52 multiple-choice questions covering all topics of the syllabus. The test will be graded by awarding 0.6 points for each correct answer, 0 points for each unanswered question, and applying a penalty of -0.15 points for each incorrect answer.
The written test will assess detailed knowledge of the functional properties of macromolecules and metabolic reactions, including the chemical structures of the compounds involved, the mechanisms regulating these reactions, and the integration of metabolism among the different tissues of the organism.
After passing the written test, students are given the opportunity to take an oral examination covering all course topics. The oral exam aims to evaluate the level of subject knowledge as well as the ability to make connections and integrate knowledge, also in relation to the future medical profession. The oral exam will also assess the student’s communication skills and appropriate use of scientific terminology. - Extended program
- BIOLOGICAL MEMBRANES. Review of lipids and biological membranes. Membrane transport: transmembrane proteins (structural properties), thermodynamics of transport, simple diffusion, facilitated transport (GLUT transporters, chloride–bicarbonate exchanger, K¿ channels, aquaporins), primary active transport (Na¿/K¿ pump, SERCA pump, ABC transporters), secondary active transport. Biosignaling: general features; GPCRs (Gs, Gi, Gq; signal transduction and termination), receptor tyrosine kinases (mechanism of action and signal termination), cyclic GMP, nitric oxide (NO), second messengers derived from phosphatidylcholine and sphingomyelin, steroid hormone receptors (mechanism of action).
BIOENERGETICS. Review of ATP structure. Introduction to metabolism: general features of metabolism (catabolism and anabolism), thermodynamics of metabolic processes, energetic role of ATP and its additional functions. Substrate-level phosphorylation: 1,3-bisphosphoglycerate, phosphocreatine, phosphoenolpyruvate, succinyl-CoA, thermodynamic aspects. Oxidative phosphorylation: redox reactions, oxidation states of carbon, electron transport chain (structure and function of respiratory chain complexes), reactive oxygen species, oxidative stress and antioxidant defenses (GSH), chemiosmotic coupling, ATP synthase (structure and mechanism of rotational catalysis), thermodynamic and quantitative aspects, regulation of oxidative phosphorylation, inhibitors and uncoupling agents. - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- 3: Health and well-being.
4: Quality education