Duration
20h Th, 10h Pr
Number of credits
| Master in bio-informatics and modelling (120 ECTS) | 3 crédits |
Lecturer
Coordinator
Language(s) of instruction
French language
Organisation and examination
Teaching in the first semester, review in January
Units courses prerequisite and corequisite
Prerequisite or corequisite units are presented within each program
Learning unit contents
The aim of this course is to present a series of techniques used to investigate the structure of proteins. It is divided in three parts: X-ray Crystallography, Nuclear Magnetic Resonance and Mass spectrometry. Each part is divided in theoretical and practical sections of similar importance.
I- X-ray diffraction (P. Charlier)
Theoretical part: 1- Overview of the crystallographic technique, 2- Macromolecular assemblies, 3- Viral capsides and ribosomal particles structures
Practical part: PYMOL tutorials for protein structures visualization and analysis.
II- Nuclear Magnetic Resonance (C. Damblon)
Theoretical part: 1- Overview of the NMR technique, 2- Structure determination.
II- Mass spectrometry (E. De Pauw)
Learning outcomes of the learning unit
This course gives to the future bioinformaticians the bases necessary to understand the principles of determination of 3D protein structure by X-ray crystallography, nuclear magnetic resonance and mass spectrometry in order to enable them to make an objective use of the models. It gives them an outline of the capacities and limits of various techniques.
Prerequisite knowledge and skills
Course of physics of 1st cycle. Basic knowledge in X-ray crystallography. Good knowledge of the basic principles of the structures of proteins. Biophysical course.
Planned learning activities and teaching methods
Tutorials dedicated to the Pymol software use: obseravtion and analysis of macromolecules structures. Use of PDB database.
Mode of delivery (face-to-face ; distance-learning)
To be decided in concertation with the different lecturers.
Recommended or required readings
The PowerPoint presentations of the theoretical course will be available on CD as well as the notes of practical works. Books recommended: - "Crystallography made hook clear: With guide for users for macromolecular models." Scale Rhodos, Academic Press 2000 - "Introduction to Protein Structure" Carl Branden and John Tooze, Garland Publishing 1999 CD roms: - PS ² and Kinemage Supplement to "Introduction to Protein Structure" Carl Branden and John Tooze, Garland Publishing 1999
Assessment methods and criteria
To be decided in concertation with the different lecturers. Most probably on the basis of a research article.
Work placement(s)
Organizational remarks
Contacts
Paulette Charlier, PhD, Chargé de CoursCristallographie des macromolécules biologiques, Centre d'Ingénierie des Protéines, Département des Sciences de la Vie, Université de Liège, Institut de Physique, B5a, B-4000 Liège, Belgium
Tel: +32 (0)4 366 36 19
Fax: +32 (0)4 366 49 54
E-mail : Paulette.Charlier@ulg.ac.be
http://www.cip.ulg.ac.be/
DAMBLON Christian
Département de chimie (sciences) / Chimie biologique structurale
Bât. B6 Chimie biologique structurale
allée du 6 Août 3
4000 Liège 1
Belgique
Tél. ULg +32 4 3663788
Fax ULg +32 4 3664577
c.damblon@ulg.ac.be
Prof. De Pauw Edwin, Dean of Chemistry Department
Mass spectrometry Laboratory
CART/GIGAproteomics
Liege University
B4000 Liege Belgium
tel direct line: +3243663415
tel secretary: +3243663414
fax: +3243663413
e.depauw@ulg.ac.be
http://www.mslab.ulg.ac.be/
http://www.giga.ulg.ac.be/