University of Liege | Version française
Study programmes 2008-2009Last update : 29/06/2009
CHIM0433-1  Proteomics
Duration :  20h Th, 10h Pr
Credits/ECTS :  
Master in Biomedicine, Research Focus, 1st yearDeuxième quadrimestre3
Master in Biomedicine, Professional Focus in Quality Assurance, 1st yearDeuxième quadrimestre3
Master en sciences biomédicales à finalité spécialisée en cosmétologie, 1st yearDeuxième quadrimestre3
Master in BiomedicineDeuxième quadrimestre3
Advanced Master in NanotechnologyToute l'année3
Holder(s) :  Edwin De Pauw, Marianne Fillet, Pierre Leprince
Language :  Langue française
Course contents :  A course on modern proteomics covering the following parts:
- Comparative protemic analysis
- Clinical proteomics
- Mass spectrometry
Course objective :  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 proteomics platform at GIGA+2 (B24)

Proteomics: Partim 3, Mass Spectrometry (Edwin De Pauw) :
- The grounds of mass spectropmetry
- Ion sources: ESI, MALDI
- Mass spectrometers according to the needs
- Separation methods and coupling with ion sources (ESI, MALDI)
- Proteins identification (bottom up, top down)
- Relative and absolute quantification using isotopic labelling, label free quantitation
- Strctural methods on intact proteins: ECD, EDD, IRMPD, H/D exchange, ion mobility
- Non-covalent complexes

A two hours practical demonstration will be held in the mass spectrometry laboratory.
Workshops :  Three 2h demonstrations in the laboratories at CHU and GIGA
Organization :  Course is composed of three 10h parts
Written notes :  available in pdf format on MyULg
Assessment :  oral examination
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


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