BIOC0715-1

Duration

25h Th, 25h Pr

Number of credits

	Master in biochemistry and molecular and cell biology (120 ECTS)	5 crédits

Lecturer

Paulette Charlier, Mireille Dumoulin

Coordinator

Paulette Charlier

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 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: Cristallogenesis, x-ray diffraction data collection, structure solution and refinement.
II - M. Dumoulin Theoretical part:
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.

Learning outcomes of the learning unit

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.

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 cristallization, the RX diffraction techniques and protein structure determination
Practicals 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.

Mode of delivery (face-to-face ; distance-learning)

One thematic week during the first quadrimester.

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 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

Proteins structure and function