Gunnar Jeschke: Catalogue data in Spring Semester 2021
|Prof. Dr. Gunnar Jeschke
|Electron Paramagnetic Resonance
Inst. Mol. Phys. Wiss.
ETH Zürich, HCI F 227
|+41 44 632 57 02
|Chemistry and Applied Biosciences
|Physical Chemistry IV: Magnetic Resonance
Enrolment ONLY for MSc students with a decree declaring this course unit as an additional admission requirement.
Any other students (e.g. incoming exchange students, doctoral students) CANNOT enrol for this course unit.
|B. H. Meier, M. Ernst, G. Jeschke
|Theoretical foundations of magnetic resonance (NMR,EPR) and selected applications.
|Introduction to magnetic resonance in isotropic and anisotropic phase.
|The course gives an introduction to magnetic resonance spectroscopy (NMR and EPR) in liquid, liquid crystalline and solid phase. It starts from a classical description in the framework of the Bloch equations. The implications of chemical exchange are studied and two-dimensional exchange spectroscopy is introduced. An introduction to Fourier spectroscopy in one and two dimensions is given and simple 'pulse trickery' is described. A quantum-mechanical description of magnetic resonance experiments is introduced and the spin Hamiltonian is derived. The chemical shift term as well as the scalar, dipolar and quadrupolar terms are discussed. The product-operator formalism is introduced and various experiments are described, e.g. polarization transfer. Applications in chemistry, biology, physics and medicine, e.g. determination of 3D molecular structure of dissolved molecules, determination of the structure of paramagnetic compounds and imaging (MRI) are presented.
|handed out in the lecture (in english)
|B. H. Meier, A. Barnes, M. Ernst, P. H. Hünenberger, G. Jeschke, F. Merkt, M. Reiher, J. Richardson, R. Riek, S. Riniker, T. Schmidt, R. Signorell, H. J. Wörner
|Seminar series covering current developments in Physical Chemistry
|Discussing current developments in Physical Chemistry
|Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR
|F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
|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.
|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.
|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
|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.