Gunnar Jeschke: Catalogue data in Spring Semester 2019 |
Name | Prof. Dr. Gunnar Jeschke |
Field | Electron Paramagnetic Resonance |
Address | Inst. Mol. Phys. Wiss. ETH Zürich, HCI F 227 Vladimir-Prelog-Weg 1-5/10 8093 Zürich SWITZERLAND |
Telephone | +41 44 632 57 02 |
gunnar.jeschke@phys.chem.ethz.ch | |
Department | Chemistry and Applied Biosciences |
Relationship | Full Professor |
Number | Title | ECTS | Hours | Lecturers | |
---|---|---|---|---|---|
529-0499-00L | Physical Chemistry | 1 credit | 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 | |
Abstract | Seminar series covering current developments in Physical Chemistry | ||||
Learning objective | |||||
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. | ||||
Learning 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. |