Gunnar Jeschke: Katalogdaten im Frühjahrssemester 2018 |
| Name | Herr Prof. Dr. Gunnar Jeschke |
| Lehrgebiet | Elektronenspinresonanz |
| Adresse | Inst. Mol. Phys. Wiss. ETH Zürich, HCI F 227 Vladimir-Prelog-Weg 1-5/10 8093 Zürich SWITZERLAND |
| Telefon | +41 44 632 57 02 |
| gunnar.jeschke@phys.chem.ethz.ch | |
| Departement | Chemie und Angewandte Biowissenschaften |
| Beziehung | Ordentlicher Professor |
| Nummer | Titel | ECTS | Umfang | Dozierende | |
|---|---|---|---|---|---|
| 529-0499-00L | Physical Chemistry | 1 KP | 1K | B. H. Meier, M. Ernst, P. H. Hünenberger, G. Jeschke, F. Merkt, M. Reiher, J. Richardson, R. Riek, S. Riniker, T. Schmidt, R. Signorell, H. J. Wörner | |
| Kurzbeschreibung | Seminarreihe über aktuelle Probleme in der Physikalischen Chemie | ||||
| Lernziel | |||||
| 551-1414-00L | Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR | 4 KP | 2V | F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich | |
| Kurzbeschreibung | The 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. | ||||
| Lernziel | Insight 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. | ||||
| Inhalt | Part 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 | ||||
| Literatur | 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. | ||||