Studying at the University of Verona
Here you can find information on the organisational aspects of the Programme, lecture timetables, learning activities and useful contact details for your time at the University, from enrolment to graduation.
Academic calendar
The academic calendar shows the deadlines and scheduled events that are relevant to students, teaching and technical-administrative staff of the University. Public holidays and University closures are also indicated. The academic year normally begins on 1 October each year and ends on 30 September of the following year.
Course calendar
The Academic Calendar sets out the degree programme lecture and exam timetables, as well as the relevant university closure dates..
Period | From | To |
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I semestre | Oct 1, 2019 | Jan 31, 2020 |
II semestre | Mar 2, 2020 | Jun 12, 2020 |
Session | From | To |
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Sessione invernale d'esame | Feb 3, 2020 | Feb 28, 2020 |
Sessione estiva d'esame | Jun 15, 2020 | Jul 31, 2020 |
Sessione autunnale d'esame | Sep 1, 2020 | Sep 30, 2020 |
Session | From | To |
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Sessione estiva di laurea | Jul 17, 2020 | Jul 17, 2020 |
Sessione autunnale di laurea | Oct 13, 2020 | Oct 13, 2020 |
Sessione autunnale di laurea - Dicembre | Dec 9, 2020 | Dec 9, 2020 |
Sessione invernale di laurea | Mar 10, 2021 | Mar 10, 2021 |
Period | From | To |
---|---|---|
Festa di Ognissanti | Nov 1, 2019 | Nov 1, 2019 |
Festa dell'Immacolata | Dec 8, 2019 | Dec 8, 2019 |
Vacanze di Natale | Dec 23, 2019 | Jan 6, 2020 |
Vacanze di Pasqua | Apr 10, 2020 | Apr 14, 2020 |
Festa della Liberazione | Apr 25, 2020 | Apr 25, 2020 |
Festa del lavoro | May 1, 2020 | May 1, 2020 |
Festa del Santo Patrono | May 21, 2020 | May 21, 2020 |
Festa della Repubblica | Jun 2, 2020 | Jun 2, 2020 |
Vacanze estive | Aug 10, 2020 | Aug 23, 2020 |
Exam calendar
Exam dates and rounds are managed by the relevant Science and Engineering Teaching and Student Services Unit.
To view all the exam sessions available, please use the Exam dashboard on ESSE3.
If you forgot your login details or have problems logging in, please contact the relevant IT HelpDesk, or check the login details recovery web page.
Academic staff
Study Plan
The Study Plan includes all modules, teaching and learning activities that each student will need to undertake during their time at the University.
Please select your Study Plan based on your enrollment year.
1° Year
Modules | Credits | TAF | SSD |
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2° Year activated in the A.Y. 2020/2021
Modules | Credits | TAF | SSD |
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3° Year activated in the A.Y. 2021/2022
Modules | Credits | TAF | SSD |
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Modules | Credits | TAF | SSD |
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Legend | Type of training activity (TTA)
TAF (Type of Educational Activity) All courses and activities are classified into different types of educational activities, indicated by a letter.
Biochemistry and analytical biochemistry (2020/2021)
Teaching code
4S02696
Credits
12
Coordinator
Language
Italian
Also offered in courses:
- Introduction to biochemistry of the course Bachelor's degree in Bioinformatics
The teaching is organized as follows:
BIOCHIMICA ANALITICA
Credits
4
Period
See the unit page
Academic staff
See the unit page
Learning outcomes
Biochemistry is a branch of life sciences which deals with the study of chemical reactions and their organization in living cells and organisms. It takes into account the studies related to the nature of the chemical constituents of living matter, their transformations in biological systems and the energy changes associated with these transformations. Students will be guided through the course to understand the relationships between structure and function of macromolecules, and the regulatory strategies, with particular focus on metabolic pathways. The experimental activities are aimed at understanding the rationale behind the basic biochemical protocols developed to investigate the macromolecules and their functions. Pratical knowledge of basic biochemical techniques by means of lessons and experiments. Students will gain a thorough competence on the main technique used in biochemistry labs, in particular they will learn isolation, identification and structure- function relationship of macromolecules, with a focus on proteins.
Program
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MM: BIOCHIMICA
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The properties that characterize living systems Biological molecules: Hierarchy among biological molecules: simple molecules as units of complex structures Water, pH and ionic balances Amino acids Acid-base properties of amino acids. Proteins: biological functions and primary structure Peptide bond. Architecture of protein molecules The three-dimensional structure of proteins: The secondary structure: description of helices and folded sheets. Ramachandran's graphs Globular proteins: tertiary structure and functional diversity Folding models. Factors determining the secondary and tertiary structure Information and thermodynamics of the survey. Conformational diseases. Quaternary structure of proteins Lipids and membranes: Fatty acids. Triacylglycerols. Membranes: Fluid mosaic model. Membrane transport Nucleotides and nucleic acids. DNA and RNA. Properties of nucleotides. Stability and formation of the phosphodiester bond. DNA denaturation and renaturation. Enzymes: catalytic power, specificity and regulation. Enzymatic kinetics: Free energy of activation and action of catalysts. The Michaelis-Menten equation. Steady state assumption. The kinetic parameters. Linear graphic methods. Enzymatic inhibition: irreversible and reversible. Competitive and non-competitive. Control mechanisms of enzymatic activity. Oxygen transport and storage: the role of hemoglobin and myoglobin. Structure-function relationship of Mb and Hb Hemoglobin: cooperative binding and allosteria. Models for the transition to allosteria in hemoglobin: the symmetrical model and the sequential model. Homotropic and heterotropic effectors. Bioenergetics. Basic thermodynamic concepts. Entropy and free energy. The course of a reaction, the variation of standard free energy. Effect of pH and cancentration on standard free energies. The importance of coupled processes in living systems. ATP and high-energy compounds: group transfer potential. The energy charge. The metabolism. The central metabolic pathways and energy metabolism. Existence of independent degradative and biosynthetic pathways. Oxidations as a source of metabolic energy. Main metabolism control mechanisms. Glycolysis: General aspects. The importance of coupled reactions in glycolysis. reactions of glycolysis. The metabolic fates of NADH and pyruvate The cycle of tricarboxylic acids: The connection phase: the oxidative decarboxylation of pyruvate. The reactions of the cycle. The cycle of TCAs as a source of intermediates for the biosynthetic pathways. Anaplerotic reactions. Electron transport and oxidative phosphorylation: Reduction potentials. The complexes of the electron transport chain. The thermodynamic approach to the chemoosmotic coupling hypothesis. ATP synthase. Shuttle systems for the transport of cytosolic NADH into mitochondria. Gluconeogenesis, glycogen metabolism and hormonal regulation. Hormones and second messengers: cAMP and G. The beta-oxidation of fatty acids with an equal number of saturated C atoms. The pentose phosphate pathway: reactions and control. Nitrogen metabolism: Transamination reactions; Fate of the carbonaceous skeleton of amino acids; fate of the amino group; urea cycle. NUCLEIC ACIDS: how the structure carries information. Structural levels of nucleic acids (DNA, RNA). DNA denaturation. TRANSFER OF INFORMATION DNA replication. Replication enzymology: structure / function of DNA polymerases. DNA replication fidelity.
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MM: BIOCHIMICA ANALITICA
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------------------------ MM: teoria ------------------------ Protein purification Ionic properties of amino acids and proteins. Isoelectric point. Sample preparation. Methods of cell disruption and production of the initial crude extracts. Protein solubilization methods. Saline swabs. Fractionation and precipitation techniques. Filtration, dialysis, sample concentration. Spectroscopic techniques. Properties of electromagnetic radiation. Light-matter interaction. States and processes involved in the phenomena of absorption, emission and decay. Absorption spectroscopy in ultraviolet and visible. Qualitative and quantitative aspects of light absorption. Colorimetric and spectroscopic methods applied to the determination of protein concentration. Spectrophotometers. Fluorescence and emission spectroscopy. Intrinsic and extrinsic fluorophores. Green fluorescent protein Spectrofluorimeters. Fluorescence resonance energy transfer (FRET). Circular dichroism. Chromatographic techniques. Principles of chromatography. The chromatogram. Parameters that determine the chromatographic performance. Van Deemter equation. Column chromatography: ion exchange, molecular exclusion, affinity, hydrophobic interaction and their applications. Electrophoretic techniques. General principles and electrophoretic mobility. Support materials. Nucleic acid electrophoresis. Protein electrophoresis. SDS PAGE. Electrophoresis in native conditions. Protein coloring on gel. Protein blotting (western blotting). Isoelectrofocusing. Basics of: Capillary electrophoresis. Two-dimensional electrophoresis gel. ------------------------ MM: laboratorio ------------------------ 1. Determination of the concentration of an unknown protein by absorption at 280 nm and by Bradford colorimetric method. 2. Determination of the kinetic parameters, Michaelis-Menten constant, turnover number, and inhibition constant of the acid phosphatase enzyme using the Lineweaver-Burk graphical linearization method. 3. Determination of the absorption spectrum of the pyridine coenzyme NADH (reduced form) and determination of the molar extinction coefficient of NADPH. 4. Determination of the molecular weight of an unknown protein by molecular exclusion chromatography. 5. Protein separation by electrophoresis under denaturing conditions (SDS-PAGE) followed by visualization of the bands by Coomassie Blue staining 6. Transfer of proteins onto the nitrocellulose membrane by electroblotting followed by immunodetection of the proteins for the identification of one or more proteins by exploiting the specificity of binding with an antibody (WESTERN BLOT). ------------------------ MM: laboratorio ------------------------ 1. Determination of the concentration of an unknown protein by absorption at 280 nm and by Bradford colorimetric method. 2. Determination of the kinetic parameters, Michaelis-Menten constant, turnover number, and inhibition constant of the acid phosphatase enzyme using the Lineweaver-Burk graphical linearization method. 3. Determination of the absorption spectrum of the pyridine coenzyme NADH (reduced form) and determination of the molar extinction coefficient of NADPH. 4. Determination of the molecular weight of an unknown protein by molecular exclusion chromatography. 5. Protein separation by electrophoresis under denaturing conditions (SDS-PAGE) followed by visualization of the bands by Coomassie Blue staining 6. Transfer of proteins onto the nitrocellulose membrane by electroblotting followed by immunodetection of the proteins for the identification of one or more proteins by exploiting the specificity of binding with an antibody (WESTERN BLOT).
Bibliography
Author | Title | Publishing house | Year | ISBN | Notes |
---|---|---|---|---|---|
R.H.Garret; C.M. Grisham | BIOCHIMICA (Edizione 5) | Piccin | 2014 | ||
CAMPBELL M.K. FARRELL S.O. MCDOUGAL M. | BIOCHIMICA (Edizione 5) | EDISES | 2019 | ||
Loredano Pollegioni | FONDAMENTI di BIOCHIMICA (Edizione 1) | Edises | 2021 | 9788836230358 | Copertina Flessibile 57 Euro e-book 42 Euro |
M. C. Bonaccorsi di Patti, R. Contestabile, M. L. Di Salvo | Metodologie Biochimiche (Edizione 2) | Zanichelli | 2019 |
Examination Methods
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MM: BIOCHIMICA
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The objective of the exam is to verify the level of knowledge and depth of the topics of the course program and the reasoning skills developed by the student. The evaluation is expressed out of thirty (minimum grade 18). The final exam (written for Bioinformatics students) will focus on all the topics of the program. The student will have to answer a series of open-ended questions, demonstrating that they understand and be able to use the fundamental concepts of each topic. The final exam (oral for Biotechnology students) will focus on all the topics of the program. The student will have to answer a series of questions, demonstrating that they understand and be able to use the fundamental concepts of each topic.
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MM: BIOCHIMICA ANALITICA
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------------------------ MM: teoria ------------------------ The final (written) exam will focus on all the topics of the program. The student will have to demonstrate that they understand and be able to use the fundamental concepts of each topic. ------------------------ MM: laboratorio ------------------------ The written exam of Analytical Biochemistry will contain questions related to laboratory experiences ------------------------ MM: laboratorio ------------------------ The written exam of Analytical Biochemistry will contain questions related to laboratory experiences
Type D and Type F activities
years | Modules | TAF | Teacher |
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3° | Python programming language | D |
Maurizio Boscaini
(Coordinator)
|
3° | Model organism in biotechnology research | D |
Andrea Vettori
(Coordinator)
|
years | Modules | TAF | Teacher |
---|---|---|---|
3° | LaTeX Language | D |
Enrico Gregorio
(Coordinator)
|
Career prospects
Module/Programme news
News for students
There you will find information, resources and services useful during your time at the University (Student’s exam record, your study plan on ESSE3, Distance Learning courses, university email account, office forms, administrative procedures, etc.). You can log into MyUnivr with your GIA login details: only in this way will you be able to receive notification of all the notices from your teachers and your secretariat via email and also via the Univr app.
Graduation
List of thesis proposals
theses proposals | Research area |
---|---|
Studio delle proprietà di luminescenza di lantanidi in matrici proteiche | Synthetic Chemistry and Materials: Materials synthesis, structure-properties relations, functional and advanced materials, molecular architecture, organic chemistry - Colloid chemistry |
Multifunctional organic-inorganic hybrid nanomaterials for applications in Biotechnology and Green Chemistry | Synthetic Chemistry and Materials: Materials synthesis, structure-properties relations, functional and advanced materials, molecular architecture, organic chemistry - New materials: oxides, alloys, composite, organic-inorganic hybrid, nanoparticles |
Dinamiche della metilazione del DNA e loro contributo durante il processo di maturazione della bacca di vite. | Various topics |
Il problema della donazione degli organi | Various topics |
Risposte trascrittomiche a sollecitazioni ambientali in vite | Various topics |
Studio delle basi genomico-funzionali del processo di embriogenesi somatica in vite | Various topics |
Attendance modes and venues
As stated in the Didactic Regulations, there is no generalised obligation of attendance. Individual lecturers are, however, free to require a minimum number of hours of attendance for eligibilitỳ for the profit exam of the teaching they teach. In such cases, attendance of teaching activities is monitored in accordance with procedures communicated in advance to students.
Part-time enrolment is permitted. Find out more on the Part-time enrolment possibilities page.
The course's teaching activities take place in the Science and Engineering area, which is composed of the buildings of Ca‘ Vignal 1, Ca’ Vignal 2, Ca' Vignal 3 and Piramide, located in the Borgo Roma cluster, and Villa Lebrecht and Villa Eugenia located in the San Floriano di Valpolicella cluster.
Lectures are held in the classrooms of Ca‘ Vignal 1, Ca’ Vignal 2 and Ca' Vignal 3, while practical exercises take place in the teaching laboratories dedicated to the various activities.