Unit CHEMISTRY AND BIOCHEMISTRY I
- Course
- Medicine and surgery
- Study-unit Code
- GP001247
- Curriculum
- In all curricula
- CFU
- 11
- Course Regulation
- Coorte 2024
- Offered
- 2024/25
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa integrata
BIOCHEMISTRY I - MOD. 1
| Code | GP001280 |
|---|---|
| CFU | 3 |
| Learning activities | Base |
| Area | Struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 3
- Teacher
- Ilaria Bellezza
- Teachers
- Ilaria Bellezza
- Hours
- 37.5 ore - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Structural biochemistry: carbohydrates, lipids, nucleotides, nucleic acids, amino acids, proteins. Hemoglobin and myoglobin
- Reference texts
- I principi di Biochimica del Lehninger - Nelson, Cox, Zanichelli
Biochimica
Berg, Tymoczko, Stryer
Zanichelli
Biochimica Medica
Siliprandi, Tettamanti
Piccin - Educational objectives
- The main competence will be to have a general knowledge necessary to address the lessons of Module 2.
- Prerequisites
- The student must have acquired basic knowledge of the main topics of General Chemistry and Organic Chemistry
- Teaching methods
- The course is organized in frontal lessons and theoretical practical lessons
- Other information
- The attendance is compulsory at least 70% of lessons. Perugia –School of Medicine – Educational and Scientific Center
- Learning verification modality
- The final examination consists of a written test and an oral exam. The written test consists of 30 multiple-choice questions relating to any topic covered in the program. For each question 4 possible answers are available of which only one is always correct. Each question is awarded 1 mark if answered correctly and 0 marks if answered incorrectly. The minimum mark for passing the written test is 18/30.
Passing the written test is compulsory for access to the oral exam but its evaluation does not contribute to the definition of the final mark.
The oral examination, lasting an average of 30 minutes, will cover all the topics discussed during the course. Knowledge of the chemical formulae of the metabolites, enzymatic reactions and their regulation are required.
During the oral examination, the student's ability to critically link different topics and the ability to express themselves in precise and clear technical language will be assessed. - Extended program
- Monosaccharides, monosaccharide cyclization, monosaccharide reactions, glycosidic bonding, oligosaccharides (sucrose, lactose, maltose), polysaccharides (glycogen, starch, cellulose, inulin), glycosaminoglycans (ac. hyaluronan, heparan sulfate, dermatan sulfate, chondroitin sulfate), Glycoconjugates (glycoproteins, proteoglycans, glycolipids).
Nucleotides, Nucleosides, phosphodiester binding, DNA-RNA stability, DNA structure, RNA structure, DNA-RNA differences, ATP functions.
Fatty acids (nomenclature, structure and properties), triacylglycerols (structure and properties), glycerophospholipids (structure and properties), dipalmitoylphosphatidylcholine, cardiolipin, glycerophosphatidylinositol, sphingolipids (sphingomyelins, gangliosides), sterols, isoprenoid derivatives, arachidonic acid derivatives. Amino acids (structure and properties), amino acid titration curves, peptide bonding (structure and properties), secondary structures: alpha-helix, sheet-beta, beta turn (structure and properties), three-dimensional structure of proteins and bonds that stabilize it. Fibrous proteins. Collagen: structure, function, post-translational modifications, hydroxylation of Pro and Lys, cross-links, collagen-associated diseases, role of vitamin C. Alpha-keratin (structure and function), myosin (structure and function). Structural motifs (helix-loop-helix, leucine zipper, zinc finger), structural domains (TIM barrel, head-tail barrel, beta sandwich), quaternary structure. Folding: thermodynamics, kinetics, protein aggregation, HSP (60, 70, 90), protein disulfide isomerase, peptidyl-prolyl isomerase.
Hemoglobin and myoglobin. Heme group (structure hints, polypeptide chain binding, function), myoglobin structure, saturation curve, myoglobin structure, conformational states, saturation curve, allosteric modulators (O2, CO2, H+, 2,3, BPG). CO2 transport. HbF, HbS, methemoglobinemia.
Actin and myosin, structure, mechanism of muscle contraction. - Obiettivi Agenda 2030 per lo sviluppo sostenibile
Cognomi M-Z
- CFU
- 3
- Teacher
- Ilaria Bellezza
- Teachers
- Ilaria Bellezza
- Hours
- 37.5 ore - Ilaria Bellezza
- Language of instruction
- Italian
- Contents
- Structural biochemistry: carbohydrates, lipids, nucleotides, nucleic acids, amino acids, proteins. Hemoglobin and myoglobin
- Reference texts
- I principi di Biochimica del Lehninger - Nelson, Cox, Zanichelli
Biochimica
Berg, Tymoczko, Stryer
Zanichelli
Biochimica Medica
Siliprandi, Tettamanti
Piccin - Educational objectives
- The main competence will be to have a general knowledge necessary to address the lessons of Module 2.
- Prerequisites
- The student must have acquired basic knowledge of the main topics of General Chemistry and Organic Chemistry
- Teaching methods
- The course is organized in frontal lessons and theoretical practical lessons
- Other information
- The attendance is compulsory at least 70% of lessons. Perugia –School of Medicine – Educational and Scientific Center
- Learning verification modality
- The final examination consists of a written test and an oral exam. The written test consists of 30 multiple-choice questions relating to any topic covered in the program. For each question 4 possible answers are available of which only one is always correct. Each question is awarded 1 mark if answered correctly and 0 marks if answered incorrectly. The minimum mark for passing the written test is 18/30.
Passing the written test is compulsory for access to the oral exam but its evaluation does not contribute to the definition of the final mark.
The oral examination, lasting an average of 30 minutes, will cover all the topics discussed during the course. Knowledge of the chemical formulae of the metabolites, enzymatic reactions and their regulation are required.
During the oral examination, the student's ability to critically link different topics and the ability to express themselves in precise and clear technical language will be assessed. - Extended program
- Monosaccharides, monosaccharide cyclization, monosaccharide reactions, glycosidic bonding, oligosaccharides (sucrose, lactose, maltose), polysaccharides (glycogen, starch, cellulose, inulin), glycosaminoglycans (ac. hyaluronan, heparan sulfate, dermatan sulfate, chondroitin sulfate), Glycoconjugates (glycoproteins, proteoglycans, glycolipids).
Nucleotides, Nucleosides, phosphodiester binding, DNA-RNA stability, DNA structure, RNA structure, DNA-RNA differences, ATP functions.
Fatty acids (nomenclature, structure and properties), triacylglycerols (structure and properties), glycerophospholipids (structure and properties), dipalmitoylphosphatidylcholine, cardiolipin, glycerophosphatidylinositol, sphingolipids (sphingomyelins, gangliosides), sterols, isoprenoid derivatives, arachidonic acid derivatives. Amino acids (structure and properties), amino acid titration curves, peptide bonding (structure and properties), secondary structures: alpha-helix, sheet-beta, beta turn (structure and properties), three-dimensional structure of proteins and bonds that stabilize it. Fibrous proteins. Collagen: structure, function, post-translational modifications, hydroxylation of Pro and Lys, cross-links, collagen-associated diseases, role of vitamin C. Alpha-keratin (structure and function), myosin (structure and function). Structural motifs (helix-loop-helix, leucine zipper, zinc finger), structural domains (TIM barrel, head-tail barrel, beta sandwich), quaternary structure. Folding: thermodynamics, kinetics, protein aggregation, HSP (60, 70, 90), protein disulfide isomerase, peptidyl-prolyl isomerase.
Hemoglobin and myoglobin. Heme group (structure hints, polypeptide chain binding, function), myoglobin structure, saturation curve, myoglobin structure, conformational states, saturation curve, allosteric modulators (O2, CO2, H+, 2,3, BPG). CO2 transport. HbF, HbS, methemoglobinemia.
Actin and myosin, structure, mechanism of muscle contraction. - Obiettivi Agenda 2030 per lo sviluppo sostenibile
BIOCHEMISTRY I - MOD. 2
| Code | GP001282 |
|---|---|
| CFU | 3 |
| Learning activities | Base |
| Area | Struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 3
- Teacher
- Davide Chiasserini
- Teachers
- Davide Chiasserini
- Hours
- 37.5 ore - Davide Chiasserini
Cognomi M-Z
- CFU
- 3
- Teacher
- Davide Chiasserini
- Teachers
- Davide Chiasserini
- Hours
- 37.5 ore - Davide Chiasserini
CHEMISTRY - MOD. 1
| Code | 50202503 |
|---|---|
| CFU | 3 |
| Learning activities | Base |
| Area | Struttura, funzione e metabolismo delle molecole d'interesse biologico |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 3
- Teacher
- Pier Luigi Orvietani
- Teachers
- Pier Luigi Orvietani
- Hours
- 37.5 ore - Pier Luigi Orvietani
Cognomi M-Z
- CFU
- 3
- Teacher
- Pier Luigi Orvietani
- Teachers
- Pier Luigi Orvietani
- Hours
- 37.5 ore - Pier Luigi Orvietani
CHEMISTRY - MOD. 2
| Code | 50202002 |
|---|---|
| CFU | 2 |
| Learning activities | Affine/integrativa |
| Area | Attività formative affini o integrative |
| Academic discipline | BIO/10 |
| Type of study-unit | Obbligatorio (Required) |
Cognomi A-L
- CFU
- 2
- Teacher
- Pier Luigi Orvietani
- Teachers
- Pier Luigi Orvietani
- Hours
- 25 ore - Pier Luigi Orvietani
Cognomi M-Z
- CFU
- 2
- Teacher
- Pier Luigi Orvietani
- Teachers
- Pier Luigi Orvietani
- Hours
- 25 ore - Pier Luigi Orvietani