Search result: Catalogue data in Spring Semester 2021
|Elective Major Subject Areas|
|Elective Major: Biological Chemistry|
|Elective Compulsory Master Courses|
|551-1402-00L||Molecular and Structural Biology VI: Biophysical Analysis of Macromolecular Mechanisms|
This course is strongly recommended for the Masters Major "Biology and Biophysics".
|W||4 credits||2V||R. Glockshuber, T. Ishikawa, S. Jonas, B. Schuler, E. Weber-Ban|
|Abstract||The course is focussed on biophysical methods for characterising conformational transitions and reaction mechanisms of proteins and biological mecromolecules, with focus on methods that have not been covered in the Biology Bachelor Curriculum.|
|Objective||The goal of the course is to give the students a broad overview on biopyhsical techniques available for studying conformational transitions and complex reaction mechanisms of biological macromolecules. The course is particularly suited for students enrolled in the Majors "Structural Biology and Biophysics", "Biochemistry" and "Chemical Biology" of the Biology MSc curriculum, as well as for MSc students of Chemistry and Interdisciplinary Natural Sciences".|
|Content||The biophysical methods covered in the course include advanced reaction kinetics, methods for the thermodynamic and kinetic analysis of protein-ligand interactions, static and dynamic light scattering, analytical ultracentrifugation, spectroscopic techniques such as fluorescence anisotropy, fluorescence resonance energy transfer (FRET) and single molecule fluorescence spectrosopy, modern electron microscopy techniques, atomic force microscopy, and isothermal and differential scanning calorimetry.|
|Lecture notes||Course material from the individual lecturers wil be made available at the sharepoint website |
|Prerequisites / Notice||Finished BSc curriculum in Biology, Chemistry or Interdisciplinary Natural Sciences. The course is also adequate for doctoral students with research projects in structural biology, biophysics, biochemistry and chemical biology.|
|529-0941-00L||Introduction to Macromolecular Chemistry||W||4 credits||3G||D. Opris|
|Abstract||Basic definitions, types of polyreactions, constitution of homo- and copolymers, networks, configurative and conformative aspects, contour length, coil formation, mobility, glass temperature, rubber elasticity, molecular weight distribution, energetics of and examples for polyreactions.|
|Objective||Understanding the significance of molecular size, constitution, configuration and conformation of synthetic and natural macromolecules for their specific physical and chemical properties.|
|Content||This introductory course on macromolecular chemistry discusses definitions, introduces types of polyreactions, and compares chain and step-growth polymerizations. It also treats the constitution of polymers, homo- and copolymers, networks, configuration and conformation of polymers. Topics of interest are contour length, coil formation, the mobility in polymers, glass temperature, rubber elasticity, molecular weight distribution, energetics of polyreactions, and examples for polyreactions (polyadditions, polycondensations, polymerizations). Selected polymerization mechanisms and procedures are discussed whenever appropriate throughout the course. Some methods of molecular weight determination are introduced.|
|Lecture notes||Course materials (consisting of personal notes and distributed paper copies) are sufficient for exam preparation.|
|Prerequisites / Notice||The course will be taught in English. Complicated expressions will also be given in German. Questions are welcome in English or German. The written examination will be in English, answers in German are acceptable. A basic chemistry knowledge is required.|
PhD students who need recognized credit points are required to pass the written exam.
|529-0242-00L||Supramolecular Chemistry||W||6 credits||3G||Y. Yamakoshi, B. M. Lewandowski|
|Abstract||Principles of molecular recognition: cation/anion complexation and their technological applications; complexation of neutral molecules in aqueous solution; non-covalent interactions involving aromatic rings; hydrogen bonding; molecular sef-assembly - a chemical approach towards nanostructures; thermodynamics and kinetics of complexation processes; synthesis of receptors; template effects.|
|Objective||The objective of this class is to reach an understanding of the nature and magnitude of the intermolecular interactions and solvation effects that provide the driving force for the association between molecules and/or ions induced by non-covalent bonding interactions. The lecture (2 h) is complemented by a problem solving class (1 h) which focuses on receptor syntheses and other synthetic aspects of supramolecular chemistry.|
|Content||Principles of molecular recognition: cation complexation, anion complexation, cation and anion complexation in technological applications, complexation of neutral molecules in aqueous solution, non-covalent interactions involving aromatic rings, hydrogen bonding, molecular sef-assembly - a chemical approach towards nanostructures, thermodynamics and kinetics of complexation processes, synthesis of receptors, template effects.|
|Lecture notes||Printed lecture notes will be available for purchase at the beginning of the class. Problem sets and answer keys will be available on-line.|
|Literature||No compulsory textbooks. Literature for further reading will be presented during the class and cited in the lecture notes.|
|Prerequisites / Notice||Course prerequisite: classes in organic and physical chemistry of the first two years of studies.|
|551-0224-00L||Advanced Proteomics |
For master students from the 2nd semester on, also doctoral candidates and post docs.
|W||4 credits||6G||P. Picotti, L. Gillet, A. Leitner, P. Pedrioli|
|Abstract||Goal of the course is to analyze current and newly emerging technologies and approaches in protein and proteome analysis with regard to their application in biology, biotechnology and medicine.|
Format: Introduction by instructor followed by discussions stimulated by reading assignments and exercises.
|Objective||To discuss current and newly emerging technologies and approaches in protein and proteome analysis with regard to their applications in biology, biotechnology, medicine and systems biology.|
|Content||Block course teaching current methods for the acquisition and processing of proteomic datasets.|
|Prerequisites / Notice||Number of people: Not exceeding 30.|
Students from ETHZ, Uni Zurich and University of Basel
Non-ETH students must register at ETH Zurich as special students http://www.rektorat.ethz.ch/students/admission/auditors/index_EN
|551-1412-00L||Molecular and Structural Biology IV: Visualizing Macromolecules by X-Ray Crystallography and EM||W||4 credits||2V||N. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, further lecturers|
|Abstract||This course provides an in-depth discussion of two main methods to determine the 3D structures of macromolecules and complexes at high resolution: X-ray crystallography and cryo-electron microscopy. Both techniques result in electron density maps that are interpreted by atomic models.|
|Objective||Students will obtain the theoretical background to understand structure determination techniques employed in X-ray crystallography and electron microscopy, including diffraction theory, crystal growth and analysis, reciprocal space calculations, interpretation of electron density, structure building and refinement as well as validation. The course will also provide an introduction into the use of cryo-electron tomography to visualize complex cellular substructures at sub-nanometer resolutions, effectively bridging the resolution gap between optical microscopy and single particle cryo-electron microscopy. Lectures will be complemented with practical sessions where students will have a chance to gain hands on experience with sample preparation, data processing and structure building and refinement.|
|Content||- History of Structural Molecular Biology|
- X-ray diffraction from macromolecular crystals
- Data collection and statistics, phasing methods
- Crystal symmetry and space groups
- X-ray data processing
- Principle of cryo-EM for biological macromolecules I, including hardware of TEM and detectors, image formation principle (phase contrast, spherical aberration, CTF), 3D reconstruction (central-section theorem, backprojection, missing information)
- Single particle analysis, including principle (projection matching, random conical tilt, angular reconstitution)
- Tomography I, including basics and subtomogram averaging
- Tomography - recent techniques, including cryo-FIB
- EM specimen preparation (cryo, negative stain), initial EM data processing
- EM and X-ray structure building, refinement, validation and interpretation
- Model building and refinement
|551-1414-00L||Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR||W||4 credits||2V||F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich|
|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
|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.
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