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.

This information is intended exclusively for students already enrolled in this course.
If you are a new student interested in enrolling, you can find information about the course of study on the course page:

Laurea magistrale in Biotecnologie agro-alimentari - Enrollment from 2025/2026

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.

CURRICULUM TIPO:

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.




S Placements in companies, public or private institutions and professional associations

Teaching code

4S02774

Credits

9

Coordinator

Daniela Cecconi

Language

Italian

Also offered in courses:

  • Proteomics of the course Masters in Molecular and Industrial Biotechniques

The teaching is organized as follows:

PROTEOMICA

Credits

3

Period

1st Semester

Academic staff

Daniela Cecconi

GENOMICA E TRASCRITTOMICA

Credits

3

Period

See the unit page

Academic staff

See the unit page

METABOLOMICA

Credits

3

Period

See the unit page

Academic staff

See the unit page

Learning outcomes

Module: GENOMICA E TRASCRITTOMICA
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Module: PROTEOMICA
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Advanced proteomic: comprehensive program focused on the concepts and technologies for studying the proteome, including the innovative new tools.


Module: METABOLOMICA
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Program

Module: GENOMICA E TRASCRITTOMICA
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Module: PROTEOMICA
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1. Introduction. The “Omics” sciences. Expressional, Functional, and Structural Proteomics.
2. Chromatographic methods (bi and multi dimensional) applied to proteome analysis. Multidimensional protein identification technology (MudPIT) and MultiDimensional Liquid Chromatography (MDLC).
3. Electrophoretic methods for proteome analysis. Isoelectrofocusing (carrier ampholytes IEF, and immobilized pH gradient, IPG). Polyacrylamide gel electrophoresis, PAGE (SDS-, Native-, and Gradient-PAGE). Two dimensional maps.
4. Sample preparation for proteomic analysis. Cell disruption, removal of interfering substances, protein solubilization, and protein quantification.
5. Pre-fractionation of the sample for the proteome analysis of low abundance proteins. Dynamic range. Differential centrifugation; immunoprecipitation; multi-step extraction of protein; affinity removal (albumin depletion, and Protein Equalizer Technology); and isoelectric focusing based fractionation (Rotofor, and Multi-compartment electrolyzer).
6. Image analysis: PDQuest and other softwares. Comparative proteomic analysis.
7. Mass spectrometry analysis. Mass spectra. Hard (electron impact EI) and soft ionization methods (chemical ionization CI, fast atom bombardment FAB, matrix assisted laser desorption ionization MALDI, and electrospray ionization ESI). Analyzers (magnetic sectors, quadrupole Q, time-of-flight TOF, ion trap IT, and Fourier Transform ion cyclotron resonance FT ICR). Detectors.
8. Tandem mass spectrometry MS/MS. Fragmenting a peptide. Tandem-in-space approach (TripleQ, Q-TOF, and TOF/TOF). Tandem-in-time approach (MALDI-TOF post source decay PSD, and IT).
9. Analysis of mass spectra. Data Base searching softwares and Data Bases for protein identification. Peptide Mass Fingerprinting (PMF), and Tandem MS data.
10. Quantitative proteomic analysis: Difference gel electrophoresis (DIGE), minimal and saturation labeling; stable isotope labeling by amino acid in cell culture (SILAC); isotope coded affinity tags (ICAT); isobaric tags for relative and absolute quantification (iTRAQ); absolute quantification (AQUA); acrylamide d0/d3; enzymatic labeling (H218O/ H216O); label free quantification (surface enhanced laser desorption/ionization SELDI-MS).
11. Post-translational modifications characterization. Glycosylation, nitration and nitrosylation, and phosphorylation. (IMAC; immunoprecipitation; biotin-switch, and other approaches).
12. Applications of proteomic analysis.


Module: METABOLOMICA
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Examination Methods

Module: GENOMICA E TRASCRITTOMICA
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Module: PROTEOMICA
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written


Module: METABOLOMICA
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Students with disabilities or specific learning disorders (SLD), who intend to request the adaptation of the exam, must follow the instructions given HERE