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| Version 2013-2014 |
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| BIOC0718-2 | Structure-function of biomolecules
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| Duration : | 25h Pr, 15h Th |
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| Number of credits : |
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| Lecturer : | Mireille Dumoulin |
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| Coordinator : | Mireille Dumoulin |
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Language(s) of instruction :
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| French language |
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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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Prerequisites and co-requisites/ Recommended optional programme components :
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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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