Frédéric Allain: Katalogdaten im Frühjahrssemester 2020
|Herr Prof. Dr. Frédéric Allain
Institut für Biochemie
ETH Zürich, HPP L 14.1
|+41 44 633 39 40
|+41 44 633 12 94
|Molecular and Structural Biology II: Molecular Machines and Cellular Assemblies
D-BIOL students are obliged to take part I and part II as a two-semester course.
|N. Ban, F. Allain, S. Jonas, M. Pilhofer
|This course on advanced topics in Molecular Biology and Biochemistry will cover the structure and function of cellular assemblies. General topics in basic biochemistry will be further developed with examples of the function of large cellular machines involved in DNA packaging, translation, virus architecture, RNA processing, cell-cell interactions, and the molecular basis of CRISPER systems.
|Students will gain a deep understanding of large cellular assemblies and the structure-function relationships governing their function in fundamental cellular processes. The lectures throughout the course will be complemented by exercises and discussions of original research examples to provide students with a deeper understanding of the subjects and to encourage active student participation.
|Advanced class covering the state of the research in structural molecular biology of basic cellular processes with emphasis on the function of large cellular assemblies.
|Updated handouts will be provided during the class.
|The lecture will be based on the latest literature. Additional suggested
Branden, C., and J. Tooze, Introduction to Protein Structure, 2nd ed.
(1995). Garland, New York.
|NMR Spectroscopy in Biology
Number of participants limited to 6.
The enrolment is done by the D-BIOL study administration.
|F. Allain, A. D. Gossert, K. Wüthrich
|In this block course, students actively participate in ongoing research projects in the research groups of Profs. Allain, Wüthrich and Dr. Gossert. The students will be tutored in their experimental work by experienced postdoc students. In addition, the course includes specific lectures that provide the theoretical background for the experimental work, as well as exercises and literature work.
|The course provides first "hands on" insight into applications of NMR spectroscopy in biological sciences. The course should enable the students to understand the potential and limitations of NMR applied to biological problems.
|The topics include studies of proteins, RNA and protein-RNA interactions,
Participation in one of the following projects will be possible:
- NMR of RNA
- NMR of several protein-RNA complexes (hnRNPF, nPTB, SR proteins)
- NMR studies of protein-ligand interactions
- dynamics of protein-RNA complexes
- Segmental isotopic labeling to study multidomain proteins
- NMR Methods Development
|Lists of individual reading assignments will be handed out.
Number of participants limited to 16.
The enrolment is done by the D-BIOL study administration.
|S. Jonas, F. Allain, C. Beyer, U. Kutay, O. Voinnet, K. Weis
|Introduction to the diversity of current RNA-research at all levels from structural biology to systems biology using mainly model systems like S. cerevisiae (yeast), mammalian cells.
|The students will obtain an overview about the diversity of current RNA-research. They will learn to design experiments and use techniques necessary to analyze different aspects of RNA biology. Through lectures and literature seminars, they will learn about the burning questions of RNA research and discuss approaches to address these questions experimentally. In practical lab projects the students will work in one of the participating laboratories. Finally, they will learn how to present and discuss their data in an appropriate manner. Student assessment is a graded semester performance based on individual performance in the laboratory, the written exam and the project presentation.
|Relevant material from the lectures will be made available during the course via the corresponding Moodle page.
|Documentation and recommended literature will be provided at the beginning and during the course.
|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.
|Molecular Biology, Biophysics
|R. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, K. Wüthrich
|The course consists of a series of research seminars on Structural Biology and Biophysics, given by both scientists of the National Center of Competence in Research (NCCR) in Structural Biology and external speakers.
|The goal of this course is to provide doctoral and postdoctoral students with a broad overview on the most recent developments in biochemistry, structural biology and biophysics.
|Voraussetzungen / Besonderes
|Information on the individual seminars is provided on the following websites: