Search result: Catalogue data in Spring Semester 2018

Biology Master Information
Elective Major Subject Areas
Elective Major: Biological Chemistry
Elective Compulsory Master Courses
551-1402-00LMolecular and Structural Biology VI: Biophysical Analysis of Macromolecular Mechanisms
This course is strongly recommended for the Masters Major "Biology and Biophysics".
W4 credits2VR. Glockshuber, T. Ishikawa, S. Jonas, B. Schuler, E. Weber-Ban
AbstractThe 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.
ObjectiveThe 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".
ContentThe biophysical methods covered in the course include advanced reaction kinetics, methods for the thermodynamic and kinetic analysis of protein-ligand interactions, classical 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 notesCourse material from the individual lecturers wil be made available at the sharepoint website

Prerequisites / NoticeFinished 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.
529-0941-00LIntroduction to Macromolecular ChemistryW4 credits3GD. Opris
AbstractBasic 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.
ObjectiveUnderstanding the significance of molecular size, constitution, configuration and conformation of synthetic and natural macromolecules for their specific physical and chemical properties.
ContentThis 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 notesCourse materials (consisting of personal notes and distributed paper copies) are sufficient for exam preparation.
Prerequisites / NoticeThe 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.
529-0242-00LSupramolecular ChemistryW6 credits3GY. Yamakoshi, B. M. Lewandowski
AbstractPrinciples 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.
ObjectiveThe 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.
ContentPrinciples 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 notesPrinted lecture notes will be available for purchase at the beginning of the class. Problem sets and answer keys will be available on-line.
LiteratureNo compulsory textbooks. Literature for further reading will be presented during the class and cited in the lecture notes.
Prerequisites / NoticeCourse prerequisite: classes in organic and physical chemistry of the first two years of studies.
551-0224-00LAdvanced Proteomics Restricted registration - show details
For master students from the 2nd semester on, also doctoral candidates and post docs.
W4 credits6GR. Aebersold, L. Gillet, M. Gstaiger, A. Leitner, P. Pedrioli
AbstractGoal 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.
ObjectiveTo 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.
ContentBlock course teaching current methods for the acquisition and processing of proteomic datasets.
Prerequisites / NoticeNumber 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 Link
551-1412-00LMolecular and Structural Biology IV: Visualizing Macromolecules by X-ray Crystallography and EMW4 credits2VN. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich
AbstractThis 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.
ObjectiveStudents 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.
551-1414-00LMolecular and Structural Biology V: Studying Macromolecules by NMR and EPRW4 credits2VF. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
AbstractThe course provides an overview of experimental methods for the determination of structures 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 the structure determination of biological macromolecules. Practical exercises with spectra to have hands on understanding of the methodology.
ContentPart I: 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.
Part II: NMR methods for structurally characterizing RNA and protein-RNA complexes.
Part III: 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.
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