Eilika Weber-Ban: Catalogue data in Spring Semester 2015

Name Prof. Dr. Eilika Weber-Ban
Address
Inst. f. Molekularbiol.u.Biophysik
ETH Zürich, HPK E 19
Otto-Stern-Weg 5
8093 Zürich
SWITZERLAND
Telephone+41 44 633 36 78
E-maileilika@mol.biol.ethz.ch
URLhttps://weber-ban-lab.ethz.ch/
DepartmentBiology
RelationshipAdjunct Professor

NumberTitleECTSHoursLecturers
551-0438-00LProtein Folding, Assembly and Degradation Restricted registration - show details
Number of participants limited to 6
6 credits7GR. Glockshuber, E. Weber-Ban
AbstractStudents 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.
Learning objectiveThe 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.
ContentThe 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
Prerequisites / NoticeMarks will be given according to the following criteria:

- Planning, execution and documentation of experimental work
- Final report, including introduction with short overview on the relevant literature, results with figures and brief discussion (maximum: 5 pages)
- Performance in the exercises
551-1323-AALFundamentals of Biology II: Biochemistry and Molecular Biology Information
Enrolment only for MSc students who need this course as additional requirement.
4 credits11RR. Glockshuber, N. Ban, K. Locher, E. Weber-Ban
AbstractAmino acids; structure of proteins; folding; dynamics and evolution; protein purification; sugars and polysaccharides; lipids and membranes. Enzymatic catalysis. Metabolism; Gene expression and propagation of genetic information; structure of DNA; transcription; protein biosynthesis; DNA replication. Gene technology; production of recombinant proteins.
Learning objectiveKnowledge on the structural construction of biological macromolecules, principles of enyme catalysed reactions, basics of molecular genetics and protein biochemistry, basic mechanisms of metabolism and of DNA replication and gene expression.
ContentPart 1: Biomolecules; amino acids; covalent assembly of proteins; three dimensional structure of proteins; folding; dynamics and evolution of proteins; methods of protein purification; sugars and polysaccharides; lipids and membranes.
Part 2: Enzymatic catalysis: classes of enzymes; kinetics of non catalysed versus catalysed reactions. Examples for the mechanisms of enzyme catalysis.
Part 3: Metabolism: Principles of metabolic pathways in living cells; glycolysis; glycogen metabolism; mechanisms of membrane transport; citric acid cycle; electron transport and oxidative phosphorylation.
Part 4: Gene expression and propagation of genetic information; structure of DNA; DNA modifying enzymes and manupulation of nucleic acids; transcription; protein biosynthesis; DNA replication.
Part 5: Gene technology; production of recombinant proteins
Literature"Biochemistry" (Voet & Voet; Wiley & Sons, 2nd edition).
551-1402-00LBiophysics and Macromolecular Mechanisms Information
This course is strongly recommended for the Masters Major "Biology and Biophysics".
4 credits2VR. Glockshuber, T. Ishikawa, B. Schuler, D. Veprintsev, E. Weber-Ban
AbstractThe course is focussed on biophysical methods for characterising conformational transitions and reaction mechanisms of proteins and biological mecromolecules, with focus on methods that have not been covered in the Biology Bachelor Curriculum.
Learning objectiveThe goal of the course is to give the students a broad overview on biopyhsical techniques available for studying conformational transitions and complex reaction mechanisms of biological macromolecules. The course is particularly suited for students enrolled in the Majors "Structural Biology and Biophysics", "Biochemistry" and "Chemical Biology" of the Biology MSc curriculum, as well as for MSc students of Chemistry and Interdisciplinary Natural Sciences".
ContentThe biophysical methods covered in the course include advanced reaction kinetics, methods for the thermodynamic and kinetic analysis of protein-ligand interactions, classical and dynamic light scattering, analytical ultracentrifugation, spectroscopic techniques such as fluorescence anisotropy, fluorescence resonance energy transfer (FRET) and single molecule fluorescence spectrosopy, modern electron microscopy techniques, atomic force microscopy, and isothermal and differential scanning calorimetry.
Lecture notesCourse material from the individual lecturers wil be made available at the sharepoint website

https://team.biol.ethz.ch/e-learn/551-1402-00L
Prerequisites / NoticeFinished BSc curriculum in Biology, Chemistry or Interdisciplinary Natural Sciences. The course is also adequate for doctoral students with research projects in structural biology, biophysics, biochemistry and chemical biology.
551-1620-00LMolecular Biology, Biophysics1 credit1KR. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, G. Wider, K. Wüthrich
AbstractThe course consists of a series of research seminars on Structural Biology and Biophysics, given by both scientists of the National Center of Competence in Research (NCCR) in Structural Biology and external speakers.
Learning objectiveThe goal of this course is to provide doctoral and postdoctoral students with a broad overview on the most recent developments in biochemistry, structural biology and biophysics.
Prerequisites / NoticeInformation on the individual seminars is provided on the following websites:
http://www.structuralbiology.unizh.ch/events005.asp
http://www.biol.ethz.ch/dbiol-cal/index