Kurt Wüthrich: Catalogue data in Spring Semester 2021
|Name||Prof. Dr. Kurt Wüthrich|
Inst. f. Molekularbiol.u.Biophysik
ETH Zürich, HPK G 17
|Telephone||+41 44 633 24 73|
|Fax||+41 44 633 11 51|
|551-0434-00L||NMR Spectroscopy in Biology |
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
|6 credits||7P||F. Allain, A. D. Gossert, K. Wüthrich|
|Abstract||In 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.|
|Objective||The 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.|
|Content||The 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 notes||No script|
|Literature||Lists of individual reading assignments will be handed out.|
|551-1412-00L||Molecular and Structural Biology IV: Visualizing Macromolecules by X-Ray Crystallography and EM||4 credits||2V||N. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, further lecturers|
|Abstract||This 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.|
|Objective||Students 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
|551-1414-00L||Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR||4 credits||2V||F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich|
|Abstract||The 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.|
|Objective||Insight 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.|
|Content||Part 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
|Literature||1) 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.
|551-1620-00L||Molecular Biology, Biophysics||1 credit||1K||R. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, K. Wüthrich|
|Abstract||The 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.|
|Objective||The 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 / Notice||Information on the individual seminars is provided on the following websites:|