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Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR
Last Updated: 2026-06-03 00:14:04
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.
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
Resources
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.
Learning Materials (Links)
- Moodle course
- Moodle-Kurs / Moodle course
General Information
- Language
- English
- Levels
- MSC
- Frequency
- Yearly recurring
Examination
- Type
- session examination
- Mode
- written 60 minutes
- Aids
- Keine Hilfsmittel zugelassen.
Course Components
| Type | Title | Time & Place | Hours |
|---|---|---|---|
| lecture | Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR |
|
2 h weekly |