Kurt Wüthrich: Katalogdaten im Frühjahrssemester 2017

NameHerr Prof. Dr. Kurt Wüthrich
LehrgebietBiophysik
Adresse
Inst. f. Molekularbiol.u.Biophysik
ETH Zürich, HPK G 17
Otto-Stern-Weg 5
8093 Zürich
SWITZERLAND
Telefon+41 44 633 24 73
Fax+41 44 633 11 51
E-Mailkw@mol.biol.ethz.ch
DepartementBiologie
BeziehungOrdentlicher Professor

NummerTitelECTSUmfangDozierende
551-0434-00LNMR Spectroscopy in Biology Belegung eingeschränkt - Details anzeigen
Number of participants limited to 8.

The enrolment is done by the D-BIOL study administration.
6 KP7GF. Allain, A. D. Gossert, K. Wüthrich
KurzbeschreibungIn this block course, students actively participate in ongoing research projects in the research groups of Profs. Allain, Wider and Wüthrich. The students will be tutored in their experimental work by doctoral or postdoctoral students. In addition, the course includes specific lectures that provide the theoretical background for the experimental work, as well as excercises and literature work.
LernzielThe 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.
InhaltThe 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 glycoproteins
- dynamics of protein-RNA complexes
- Segmental isotopic labeling to study multidomain proteins
-Structural and dynamic properties of FtsZ, the bacterial homolog of tubulin
- investigations of the ubiquitinom
- NMR Methods Development
SkriptNo script
LiteraturLists of individual reading assignments will be handed out.
551-1412-00LMolecular and Structural Biology IV: Visualizing Macromolecules by X-ray Crystallography and EM4 KP2VN. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich
KurzbeschreibungThis 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.
LernzielStudents 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. Tentative list of topics is as follows: 1) History of Structural 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 including discussions about hardware and theory of image formation principles in EM, Single particle analysis, EM data processing, Tomography, including subtomogram averaging, EM and X-ray structure building, refinement and validation theory and practice.
551-1414-00LMolecular and Structural Biology V: Studying Macromolecules by NMR and EPR4 KP2VF. Allain, A. D. Gossert, G. Jeschke, G. Wider, K. Wüthrich
KurzbeschreibungThe course provides an overview of experimental methods for the determination of structures of macromolecules at atomic resolution in solution. The two main methods used are Nuclear Magnetic Resonance (NMR) spectroscopy and Electron Paramagnetic Resonance (EPR) spectroscopy.
LernzielInsight into the methodology, areas of application and limitations of these two methods for the structure determination of biological macromolecules. Practical exercises with spectra to have hands on understanding of the methodology.
InhaltPart I: Methods for the determination of protein structures in solution using nuclear magnetic resonance (NMR) spectroscopy. Experimental approaches to the characterization of intramolecular dynamics of proteins.
Part II: NMR methods for structurally characterizing RNA and protein-RNA complexes.
Part III: EPR of biomolecules
Literatur1) 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 KP1KR. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, K. Wüthrich
KurzbeschreibungThe 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.
LernzielThe 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.
Voraussetzungen / BesonderesInformation 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