University of Liege | Version française
Academic year 2014-2015Value date : 12/05/2015
CHIM0433-1  Proteomics

Duration :  20h Th, 10h Pr
Number of credits :  
Master in Biomedicine, Research Focus, 1st year3
Master in Biomedicine, Professional Focus in Quality Assurance, 1st year3
Master in Biomedicine, Professional Focus in focus in cosmetology, 1st year3
Master in Biomedicine3
Advanced Master in Nanotechnology3
Lecturer :  Edwin De Pauw, Marianne Fillet, Pierre Leprince
Language(s) of instruction :  
French language
Organisation and examination :  
Teaching in the second semester
Course contents :  
A course on modern proteomics covering the following parts:
- Comparative protemic analysis
- Clinical proteomics
- Mass spectrometry
Learning outcomes of the course :  
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.
Prerequisites and co-requisites/ Recommended optional programme components :  
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



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