CHIM0433-1 : Proteomics

Study Programmes 2015-2016

CHIM0433-1

Proteomics

Duration :

20h Th, 10h Pr

Number of credits :

Master in biomedicine (120 ECTS)		3
Master in biomedicine (60 ECTS)		3
Specialised master in nanotechnology		3

Lecturer :

Marianne Fillet, Pierre Leprince, Gabriel Mazzucchelli

Language(s) of instruction :

French language

Organisation and examination :

Teaching in the second semester

Units courses prerequisite and corequisite :

Prerequisite or corequisite units are presented within each program

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 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