Gunnar Jeschke: Catalogue data in Spring Semester 2023

Name Prof. Dr. Gunnar Jeschke
FieldElectron Paramagnetic Resonance
Inst. Mol. Phys. Wiss.
ETH Zürich, HCI F 227
Vladimir-Prelog-Weg 1-5/10
8093 Zürich
Telephone+41 44 632 57 02
DepartmentChemistry and Applied Biosciences
RelationshipFull Professor

529-0432-AALPhysical 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.
4 credits9RG. Jeschke, M. Ernst
AbstractTheoretical foundations of magnetic resonance (NMR,EPR) and selected applications.
ObjectiveIntroduction to magnetic resonance in isotropic and anisotropic phase.
ContentThe 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.
Lecture noteshanded out in the lecture (in english)
529-0499-00LPhysical Chemistry0 credits1KG. Jeschke, A. Barnes, M. Ernst, P. H. Hünenberger, F. Merkt, M. Reiher, J. Richardson, R. Riek, S. Riniker, T. Schmidt, R. Signorell, H. J. Wörner
AbstractSeminar series covering current developments in Physical Chemistry
ObjectiveDiscussing current developments in Physical Chemistry
529-1025-00LPhysical Chemistry (for Pharmacy)3 credits2V + 1UG. Jeschke, M. Yulikov
AbstractThermodynamic foundations of phase equilibria, intermolecular interactions, and molecular self-assembly; kinetics of chemical reactions and transport processes
ObjectiveThis course teaches physical-chemical foundations of important processes in cells and organisms as well as in galenics. Students learn:

1. Evaluation of chemical equilibria based on chemical potential

2. Interpretation of phase diagrams

3. Which interactions between molecules are important in living cells

4. Why molecules self-organize into aggregates

5. Which physical-chemical basics determine behavior of biomembranes

6. What determines the rate of chemical reactions, in particular also of enzymatically catalyzed reactions

7. What determines the transport rate of matter and heat
Contentchemical potential, prediction of the direction of processes, phase equilibria, phase rule, phase diagrams of pure substances, colligative properties, osmosis, dialysis, surface tension, intermolecular interactions, hydrophobic effect, hydrophilic effect and denaturation, amphiphiles, basics of self-association, micelles, packing parameter, double layers, vesicles, membranes, elementary reactions, parallel reactions, consecutive reactions, Eyring theory, enzyme kinetics, diffusion, heat conduction, active transport
Lecture notesElectronic lecture notes are available in Moodle and on
LiteratureIn addition to the lecture script, the following two books can be used to gain deeper understanding

Marc R. Roussel, A Life Scientist's Guide to Physical Chemistry, Cambridge University Press, 2012

Jacob Israelachvili, Intermolecular and Surface Forces, Academic Press, 1992
Prerequisites / NoticeVoraussetzungen: Physik II für Bio/Pharm. Wiss.
Subject-specific CompetenciesConcepts and Theoriesfostered
Techniques and Technologiesfostered
Method-specific CompetenciesAnalytical Competenciesfostered
Media and Digital Technologiesfostered
Project Managementfostered
Social CompetenciesCommunicationfostered
Cooperation and Teamworkfostered
Customer Orientationfostered
Leadership and Responsibilityfostered
Self-presentation and Social Influence fostered
Sensitivity to Diversityfostered
Personal CompetenciesAdaptability and Flexibilityfostered
Creative Thinkingfostered
Critical Thinkingfostered
Integrity and Work Ethicsfostered
Self-awareness and Self-reflection fostered
Self-direction and Self-management fostered
551-1414-00LMolecular and Structural Biology V: Studying Macromolecules by NMR and EPR4 credits2VF. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
AbstractThe 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.
ObjectiveInsight 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.
ContentPart 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
Literature1) 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.