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| BIOC0715-1 | Proteins structure and function
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| Duration : | 25h Th, 25h Pr |
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| Number of credits : |
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| Lecturer : | Paulette Charlier, Mireille Dumoulin |
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| Coordinator : | Paulette Charlier |
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Language(s) of instruction :
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| French language |
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Course contents :
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| The aim of this course is to present a series of techniques used to investigate the structure and the stability of proteins. It is divided in three parts: X-ray diffraction and its various applications, the amyloides fibril in various contextes and the Nuclear Magnetic Resonance. each part is divided in theoretical and practical sections of similar importance.
I- X-ray diffraction
Theoretical part: 1- Overview of the crystallographic technique, 2- High resolution structures, 3- Neutron diffraction, 4- Laue diffraction, 5- Fibers diffraction, 6- Macromolecular assemblies structures, 7- Viral capsides ribosomal particles structures
Practical part: PYMOL tutorials for protein structures visualization and analysis.
Lab visit and demonstration of protein crystals and fibers diffraction experiments.
II - Amyloid fibrils (M. Dumoulin)
Theoretical part: 1 - Formation of amyloid fibrils, 2- Amyloid fibrils and degenerative diseases, 3- Functional amyloid fibrils, 4- Amyloid fibrils and nanotechnologies
Practical part: First the structural propertties and the stability of a serie of known proteins are investigated. Then, based on these data, the nature of three unknown samples is investigated. The techniques used include: absorbancy, fluorescence, circular dichroism and electronic microscopy.
III- Nuclear Magnetic Resonance (C. Damblon)
Theoretical part: 1- Overview of the NMR technique, 2- Structure determination, 3- Protein-ligand interactions
Practical part: Data collection with a 500MHz spectrometer. |
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Learning outcomes of the course :
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| This course gives to the future biochemists the bases necessary to understand the principles of determination of 3D protein structure by X-ray crystallography and nuclear magnetic resonance 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 of X-ray crystallography and NMR.
Moreover, it will give them a description of various biospectroscopic techniques(absorbance, fluorescence, circular dichroism) to study protein stability. |
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Prerequisites and co-requisites/ Recommended optional programme components :
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| 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. |
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Planned learning activities and teaching methods :
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| Tutorials dedicated to the Pymol software use: obseravtion and analysis of macromolecules structures. Use of PDB database.
Paracticals dedicated to the study of the structure and the stability of proteins by a series of techniques including absorbancy, fluorescence, circular dichroism, electronic microscopy and NMR. |
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Mode of delivery (face-to-face ; distance-learning) :
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| One thematic week during the first quadrimester. |
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Recommended or required readings :
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| 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 |
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Assessment methods and criteria :
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| To be decided in concertation with the different lecturers. Most probably on the basis of a research article. |
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Contacts :
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| Paulette Charlier, PhD, Chargé de Cours
Cristallographie 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/
Dr. Mireille DUMOULIN
Enzymology and Protein Folding - CIP, Institute of Chemistry, Bat. B6c - Sart-Tilman, 4000 Liège
Tél. 04/366.35.46 - Fax 04/366.33.64
E-mail : mdumoulin@ulg.ac.be |
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