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551-0438-00L 6 Credits BSC D-BIOL
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Protein Folding, Assembly and Degradation

Lecturers: Prof. em. Dr. Rudolf Glockshuber, Prof. Dr. Eilika Weber-Ban
Examiners: Prof. em. Dr. Rudolf Glockshuber
Number of participants limited to 6. The enrolment is done by the D-BIOL study administration. General safety regulations for all block courses: -Whenever possible the distance rules have to be respected -All students have to wear masks throughout the course. Please keep reserve masks ready. Surgical masks (IIR) or medical grade masks (FFP2) without a valve are permitted. Community masks (fabric masks) are not allowed. -The installation and activation of the Swiss Covid-App is highly encouraged -Any additional rules for individual courses have to be respected -Students showing any COVID-19 symptoms are not allowed to enter ETH buildings and have to inform the course responsible
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Last Updated: 2026-02-05 15:53:52

Abstract

Students will carry out defined research projects related to the current research topics of the groups of Prof. Glockshuber and Prof. Weber-Ban. The topics include mechanistic studies on the assembly of adhesive pili from pathogenic bacteria, disulfide bond formation in the bacterial periplasm, ATP-dependent chaperone-protease complexes and formation of amyloid deposits in Alzheimer's disese.

Objective

The course should enable the students to understand and apply biophysical methods, in particular kinetic and spectroscopic methods, to unravel the mechanism of complex reactions of biological macromolecules and assemblies in a quantitative manner.

Content

The students will be tutored in their experimental work by doctoral or postdoctoral students from the Glockshuber or Weber-Ban group. In addition, the course includes specific lectures that provide the theoretical background for the experimental work, as well as excercises on the numeric evaluation of biophysical data, and literature work. Participation in one of the following projects will be possible: Projects of the Glockshuber group: - Purification, biophysical characterization and structure determiation of enzymes required for disulfide bond formation in the periplasm of Gram-negative bacteria. - Mechanistic studies on the assembly of type 1 pili from pathogenic Escherichia coli strains. In vitro reconstitution of pilus assembly from all purified components. Characterization of folding, stability and assembly behaviour of individual pilus subunits. - Identification of intermediates in the aggregation of the human Abeta peptide Experimental work on these projects involves - Molecular cloning, recombinant protein production in E. coli and protein purification - Protein crystallization - Thermodynamic and kinetic characterization of conformational changes in proteins and protein-ligand interactions by fluorescence and circular dischoism spectroscopy - Analysis of rapid reactions by stopped-flow fluorescence - Negative-stain electron microscopy - Light scattering Projects of the Weber-Ban group: - Generation and purification of site-directed variants of the E. coli ClpA/P protease and chaperone-proteasome complexes from other organisms, their biophysical characterization, including rapid kinetics by stopped-flow methods, ATPase activity measurtements, negative-stain electron microscopy and light scattering

General Information

Language
English
Levels
BSC
Frequency
Semesterly recurring

Examination

Type
graded semester performance
Die der Benotung des Blockkurses zugrundeliegenden Kriterien werden zu Beginn des Kurses bekanntgegeben. Es wird nur der hauptverantwortliche Examinator aufgeführt. Weitere Examinatoren: Die oben aufgeführten Dozenten.

Course Components

Type Title Time & Place Hours
practical/laboratory course Protein Folding, Assembly and Degradation
Permission from lecturers required for all students. Block course in the semester break. Monday 14. June 2021 to Tuesday 29. June 2021 Place: 14. June 2021 9:00 HPK D3
No time listed 100 h semesterly

Offered In