Kaspar Locher: Catalogue data in Spring Semester 2015 |
| Name | Prof. Dr. Kaspar Locher |
| Field | Molecular Membrane Biology |
| Address | Inst. f. Molekularbiol.u.Biophysik ETH Zürich, HPK G 11 Otto-Stern-Weg 5 8093 Zürich SWITZERLAND |
| Telephone | +41 44 633 39 91 |
| locher@mol.biol.ethz.ch | |
| URL | http://www.locherlab.ethz.ch |
| Department | Biology |
| Relationship | Full Professor |
| Number | Title | ECTS | Hours | Lecturers | |
|---|---|---|---|---|---|
| 551-0142-00L | Structure Determination of Biological Macromolecules by X-ray Crystallography and NMR | 6 credits | 3G | F. Allain, N. Ban, K. Locher, G. Wider, K. Wüthrich, further lecturers | |
| Abstract | The course provides an overview of experimental methods for the determination of structures of macromolecules at atomic resolution. | ||||
| Learning objective | Insight into the methodology, areas of application and limitations of two principal methods for the structure determination of biological macromolecules. | ||||
| Content | Part I: Methods for the determination of the structure of proteins and macromolecular complexes using X-ray diffraction in single crystals. Part II: Methods for the determination of protein structures in solution using nuclear magnetic resonance (NMR) spectroscopy. Experimental approaches to the characterization of intramolecular dynamics of proteins. | ||||
| Literature | 1) Wüthrich, K. NMR of Proteins and Nucleic Acids, Wiley-Interscience. 2) Blow, D. Outline of Crystallography for Biologists. Oxford University Press. | ||||
| 551-1323-AAL | Fundamentals of Biology II: Biochemistry and Molecular Biology  Enrolment only for MSc students who need this course as additional requirement. | 4 credits | 11R | R. Glockshuber, N. Ban, K. Locher, E. Weber-Ban | |
| Abstract | Amino acids; structure of proteins; folding; dynamics and evolution; protein purification; sugars and polysaccharides; lipids and membranes. Enzymatic catalysis. Metabolism; Gene expression and propagation of genetic information; structure of DNA; transcription; protein biosynthesis; DNA replication. Gene technology; production of recombinant proteins. | ||||
| Learning objective | Knowledge on the structural construction of biological macromolecules, principles of enyme catalysed reactions, basics of molecular genetics and protein biochemistry, basic mechanisms of metabolism and of DNA replication and gene expression. | ||||
| Content | Part 1: Biomolecules; amino acids; covalent assembly of proteins; three dimensional structure of proteins; folding; dynamics and evolution of proteins; methods of protein purification; sugars and polysaccharides; lipids and membranes. Part 2: Enzymatic catalysis: classes of enzymes; kinetics of non catalysed versus catalysed reactions. Examples for the mechanisms of enzyme catalysis. Part 3: Metabolism: Principles of metabolic pathways in living cells; glycolysis; glycogen metabolism; mechanisms of membrane transport; citric acid cycle; electron transport and oxidative phosphorylation. Part 4: Gene expression and propagation of genetic information; structure of DNA; DNA modifying enzymes and manupulation of nucleic acids; transcription; protein biosynthesis; DNA replication. Part 5: Gene technology; production of recombinant proteins | ||||
| Literature | "Biochemistry" (Voet & Voet; Wiley & Sons, 2nd edition). | ||||
| 551-1556-00L | X-Ray Crystallographic Structure Determination and Biophysics  Number of participants limited to 8 per quarter | 6 credits | 7G | K. Locher, G. Schertler, D. Veprintsev | |
| Abstract | This course will familiarize the students with techniques used for the biophysical and structural characterization of proteins. The students will carry out biophysical characterization of the proteins with dynamic light scattering and CD spectroscopy. | ||||
| Learning objective | The course aims at introducing the principles of protein X-ray crystallography as well as other techniques used in the biophysical characterization of proteins. Students will get an opportunity to conduct hands-on experiments and also use computational techniques. | ||||
| Content | Micro-calorimetry and fluorescence anisotropy measurements will be used to study protein peptide interactions. The course also includes a demonstration of the Synchrotron capabilities at the Paul Scherrer Institute (SLS). Students will crystallize a protein, collect X-ray diffraction data using an in-house X-ray source, and build an atomic model into the electron density map. | ||||
| Prerequisites / Notice | The students will be both at ETH Honggerberg and the Paul Scherrer Institute (PSI) at Villigen. Transport will be organized by rental car or by public transportation. | ||||
| 551-1620-00L | Molecular Biology, Biophysics | 1 credit | 1K | R. Glockshuber, F. Allain, N. Ban, K. Locher, E. Weber-Ban, G. Wider, K. Wüthrich | |
| Abstract | 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. | ||||
| Learning objective | 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. | ||||
| Prerequisites / Notice | Information on the individual seminars is provided on the following websites: http://www.structuralbiology.unizh.ch/events005.asp http://www.biol.ethz.ch/dbiol-cal/index | ||||