Kurt Wüthrich: Catalogue data in Spring Semester 2022

Name Prof. Dr. Kurt Wüthrich
FieldBiophysik
Address
Inst. f. Molekularbiol.u.Biophysik
ETH Zürich, HPK G 17
Otto-Stern-Weg 5
8093 Zürich
SWITZERLAND
Telephone+41 44 633 24 73
Fax+41 44 633 11 51
E-mailkw@mol.biol.ethz.ch
DepartmentBiology
RelationshipFull Professor

NumberTitleECTSHoursLecturers
551-0434-00LNMR Spectroscopy in Biology Restricted registration - show details
Number of participants limited to 6.

The enrolment is done by the D-BIOL study administration.
6 credits7PF. Allain, A. D. Gossert, K. Wüthrich
AbstractIn this block course, students actively participate in ongoing research projects in the research groups of Profs. Allain, Wüthrich and Dr. Gossert. The students will be tutored in their experimental work by experienced postdoc students. In addition, the course includes specific lectures that provide the theoretical background for the experimental work, as well as exercises and literature work.
ObjectiveThe course provides first "hands on" insight into applications of NMR spectroscopy in biological sciences. The course should enable the students to understand the potential and limitations of NMR applied to biological problems.
ContentThe topics include studies of proteins, RNA and protein-RNA interactions,

Participation in one of the following projects will be possible:
- NMR of RNA
- NMR of several protein-RNA complexes (hnRNPF, nPTB, SR proteins)
- NMR studies of protein-ligand interactions
- dynamics of protein-RNA complexes
- Segmental isotopic labeling to study multidomain proteins
- NMR Methods Development
Lecture notesNo script
LiteratureLists of individual reading assignments will be handed out.
551-1412-00LMolecular and Structural Biology IV: Visualizing Macromolecules by X-Ray Crystallography and EM4 credits2VN. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, further lecturers
AbstractThis course provides an in-depth discussion of two main methods to determine the 3D structures of macromolecules and complexes at high resolution: X-ray crystallography and cryo-electron microscopy. Both techniques result in electron density maps that are interpreted by atomic models.
ObjectiveStudents will obtain the theoretical background to understand structure determination techniques employed in X-ray crystallography and electron microscopy, including diffraction theory, crystal growth and analysis, reciprocal space calculations, interpretation of electron density, structure building and refinement as well as validation. The course will also provide an introduction into the use of cryo-electron tomography to visualize complex cellular substructures at sub-nanometer resolutions, effectively bridging the resolution gap between optical microscopy and single particle cryo-electron microscopy. Lectures will be complemented with practical sessions where students will have a chance to gain hands on experience with sample preparation, data processing and structure building and refinement.
Content- History of Structural Molecular Biology

- X-ray diffraction from macromolecular crystals

- Data collection and statistics, phasing methods

- Crystal symmetry and space groups

- X-ray data processing

- Principle of cryo-EM for biological macromolecules I, including hardware of TEM and detectors, image formation principle (phase contrast, spherical aberration, CTF), 3D reconstruction (central-section theorem, backprojection, missing information)

- Single particle analysis, including principle (projection matching, random conical tilt, angular reconstitution)

- Tomography I, including basics and subtomogram averaging

- Tomography - recent techniques, including cryo-FIB
- EM specimen preparation (cryo, negative stain), initial EM data processing

- EM and X-ray structure building, refinement, validation and interpretation

- Model building and refinement
551-1414-00LMolecular and Structural Biology V: Studying Macromolecules by NMR and EPR4 credits2VF. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
AbstractThe course provides an overview of experimental methods for studying function and structure of macromolecules at atomic resolution in solution. The two main methods used are Nuclear Magnetic Resonance (NMR) spectroscopy and Electron Paramagnetic Resonance (EPR) spectroscopy.
ObjectiveInsight into the methodology, areas of application and limitations of these two methods for studying biological macromolecules. Practical exercises with spectra to have hands on understanding of the methodology.
ContentPart I: Historical overview of structural biology.
Part II: Basic concepts of NMR and initial examples of applications.
2D NMR and isotope labeling for studying protein function and molecular interactions at atomic level.
Studies of dynamic processes of proteins in solution.
Approaches to study large particles.
Methods for determination of protein structures in solution.
Part III: NMR methods for structurally characterizing RNA and protein-RNA complexes.
Part IV: EPR of biomolecules
Literature1) Wüthrich, K. NMR of Proteins and Nucleic Acids, Wiley-Interscience.
2) Dominguez et al, Prog Nucl Magn Reson Spectrosc. 2011 Feb;58(1-2):1-61.
3) Duss O et al, Methods Enzymol. 2015;558:279-331.
551-1620-00LMolecular Biology, Biophysics1 credit1KR. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, 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.
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