Study Programmes 2015-2016
| BIOC0718-2 | ||||||||
| Structure-function of biomolecules | ||||||||
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Duration :
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| 25h Pr, 15h Th | ||||||||
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Number of credits :
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Lecturer :
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| Mireille Dumoulin | ||||||||
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Coordinator :
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| Mireille Dumoulin | ||||||||
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Language(s) of instruction :
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| French language | ||||||||
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Organisation and examination :
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| Teaching in the second semester | ||||||||
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Units courses prerequisite and corequisite :
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| Prerequisite or corequisite units are presented within each program | ||||||||
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Course contents :
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| THEORETICAL PART
1- Basis of protein folding and major techniques used to investigate protein folding in vitro 2- In vivo protein folding - Main techniques used to investigate protein folding in vivo - Role of chaperones 3- Degradation of misfolded proteins (proteosome) 4- 5- Protein misfolding and diseases - Diseases associated with the loss of active protein - Diseases associated with protein aggregation (amyloid disorders, non amyloid aggregation disorders) 6- Functional amyloids - Amyloids as functional coats for microorganisms - Amyloids as orchester of the biosynthesis of melanin in mamalian tissue - Prions: proteins as genes and infectious diseases - Amyloid fibrils as nanomaterial 7- Functional glycoproteins, roles in biology. Structural glycoproteins, roles in extracellular matrix 8- Nanobodies: structure, properties and therapeutic applications 9- Toxin-antitoxin pairs in bacteria: killers or stress regulators? 10- Protein allostery, signal transmission and conformational dynamics 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. |
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Learning outcomes of the course :
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| A theoretical overview of techniques of used in studying the structure, stability and function of proteins is given. Applications include classical equiilibrium thermodynamics and spectroscopic methods including: UV-Vis spectroscopy, circular dichroism, fluorescence. | ||||||||
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Prerequisite knowledge and skills :
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Planned learning activities and teaching methods :
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Mode of delivery (face-to-face ; distance-learning) :
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Recommended or required readings :
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Assessment methods and criteria :
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| he valuation will be based on the report related to practicals | ||||||||
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Work placement(s) :
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Organizational remarks :
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| The PowerPoint presentations of the theoretical course will be available on CD as well as the notes of practical works. | ||||||||
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Contacts :
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| Mireille Dumoulin
Research Associate F.R.S.-FNRS Centre for Protein Engineering, Laboratory of Enzymology and Protein Folding Institut of Chemistry, B6 University of Liege Sart Tilman, B4000 LIEGE, Belgium Tel: 0032 (0)4 366 3546 Fax: 0032 (0)4 366 3364 |
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