2018-2019 / CHIM0433-1

Proteomics

Duration

20h Th, 10h Pr

Number of credits

 Master in biomedicine (120 ECTS)3 crédits 
 Master in biomedicine (60 ECTS)3 crédits 
 Specialised master in nanotechnology3 crédits 

Lecturer

Marianne Fillet, Pierre Leprince, Gabriel Mazzucchelli

Language(s) of instruction

French language

Organisation and examination

Teaching in the second semester

Schedule

Schedule online

Units courses prerequisite and corequisite

Prerequisite or corequisite units are presented within each program

Learning unit contents

A course on modern proteomics covering the following parts:
- Comparative protemic analysis
- Clinical proteomics
- Mass spectrometry

Learning outcomes of the learning unit

  • Proteomics, partim comparative proteomic analysis (Pierre Leprince):
- Genomics and proteomics, promises and reality - Protein chemistry facts useful for proteomic research - Classical electrophoretic analysis techniques - 2D-DIGE: principles and methods - Samples preparation and processing - Electrophoretic separation and gel analysis - Tools for gel image analysis : Decyder DIA, BVA - Spot picking and tryptic digestion - Results validation - Technical bias and limitations -Examples of comparative proteomic analysis of physiological and pathological responses
A 2h practical demonstration is taking place in the proteomics laboratory at the CNCM (B36)
 
 






  • Clinical proteomic (Marianne Fillet)
- Introduction - Novel technologies used for clinical proteomic - Sample preparation for body fluid samples - Statistical and bioinformatics tools - Identification and validation of new diseases biomarkers; - Prediction responses to therapy and diseases follow-up
A 2h practical demonstration is taking place in the laboratory for the Analysis of Medicines (Tower 4, +3, B36).
 

 





  • Proteomics: Partim Mass Spectrometry (Gabriel Mazzucchelli):
- The basics of mass spectropmetry :Ion sources ESI, MALDI - Mass analyzers : TOF, quadripole, IT, Orbitrap, FT-ICR - Mass spectrometers according to the needs - Separation methods and coupling with ion sources (ESI, MALDI) - Multidimensional mass spectrometry - Proteins identification (bottom up, top down) - de novo sequencing - Structural methods on intact proteins: ECD, EDD, IRMPD, H/D exchange, ion mobility - Relative and absolute quantification using isotopic labelling, label free quantitation - Non-covalent complexes
A two hours practical demonstration will be held in the Mass Spectrometry Laboratory (building B6c).

Prerequisite knowledge and skills

Planned learning activities and teaching methods

Three 2h demonstrations in the laboratories at CHU and GIGA

Mode of delivery (face-to-face ; distance-learning)

Course is composed of three 6.5 h parts

Recommended or required readings

available in pdf format on MyULg

Assessment methods and criteria

written examination

Work placement(s)

Organizational remarks

Contacts

Pierre Leprince
Centre for Cellular and Molecular Neurobiology (CNCM)
Université de Liège
CHU B36
B-4000 Liège
Belgique
Tél: 32 4 366 59 32
FAX: 32 4 366 59 12
pleprince@ulg.ac.be

Items online

Gel-free Proteomics
Review

Mass Spectrometry Basics 2018
Mass spectrum, sources and analysers.