Search result: Catalogue data in Spring Semester 2020

Number	Title	Type	ECTS	Hours	Lecturers
Biology Bachelor
3. Year, 6. Semester
Block Courses Registration for Block courses is mandatory. Please register under https://www.uzh.ch/zoolmed/ssl-dir/Blockkurse_UNIETH.php. Registration period from 16.12.2019 - 06.01.2020 Please note the ETH admission criteria for the admission of ETH students to ETH block courses on the block course registration website under "allocation".
Block Courses in 2nd Quarter of the Semester From 12.3.2020 to 2.4.2020
376-1346-00L	Study of Epigenetic Mechanisms in Mental Health Number of participants limited to 12. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	I. Mansuy
Abstract	This block course is focused on the study of the epigenetic mechanisms that regulate complex brain functions and behavior. It provides an overview of molecular methods used in experimental mice or in human samples to investigate epigenetic processes that control genome activity and gene expression, and are associated with cognitive functions and behavioral responses.
Learning objective	The purpose is to learn the principles of major methods in epigenetics that allow examine genome activity at the level of DNA, RNA or protein, in the context of complex brain functions.
Content	4 independent projects for 3 students each covering various aspects of epigenetic mechanisms. It will focus on state-of-the-art techniques to measure or manipulate gene expression and gene activity in the adult brain or in cell culture, and analyse the effects in vitro or in vivo using omics analyses, molecular and biochemical tools and behavioral testing.
Lecture notes	Provided at the beginning of the practical.
551-0352-00L	Introduction to Mass Spectrometry-based Proteomics Number of participants limited to 12. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	L. Gillet, P. Picotti
Abstract	Protein Analysis by Mass Spectrometry The following topics will be covered: basics of biological mass spectrometry, including instrumentation, data collection and data analysis; applications to protein identification and characterization; sample preparation methods; proteomics strategies; and quantitative analysis.
Learning objective	How to prepare a protein sample for MS analysis (trypsin digestion, C18 clean-up) Principles of data acquisition LC-MS (QTOF and/or Ion Trap instruments) Perform qualitative proteomic analysis (protein identification with Mascot and/or Sequest Softwares) Perform quantitative proteomic analysis (label-free and labeled analyses) Analyze/interpret the data to find up/down regulated proteins
551-0434-00L	NMR Spectroscopy in Biology Number of participants limited to 6. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	F. Allain, A. D. Gossert, K. Wüthrich
Abstract	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.
Learning objective	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.
Content	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
Lecture notes	No script
Literature	Lists of individual reading assignments will be handed out.
529-0810-01L	Laboratory Course Organic Chemistry II (for D-BIOL) Number of participants limited to 12. Please contact Prof. C. Thilgen (thilgen@org.chem.ethz.ch) as early as possible, end of Autumn Semester. You will get a confirmation if you are accepted. The enrolment is done by the D-BIOL study administration. The de-facto language of instruction depends on the tutor.	W	12 credits	4P	C. Thilgen
Abstract	An organic-synthetic sub-project of the current research of a group from the Laboratory of Organic Chemistry is carried out under the guidance of doctoral students.
Learning objective	Learn to plan and carry out challenging multistep syntheses making use of modern methods; reach a deeper understanding of organic reactions through experimental work; develop an organic-synthetic research project; take accurate notes, write a publication style report, and present the obtained results in a seminar.
Content	An organic-synthetic sub-project of the current research of a group from the Laboratory of Organic Chemistry is carried out under the guidance of doctoral students.
Lecture notes	No course notes.
Literature	No set textbooks. Literature will be indicated or provided by the supervising TAs.
Prerequisites / Notice	Course prerequisites: Accomplished laboratory course Organic Chemistry I (529-0229-00) and passed session exam Organic Chemistry I (529-0221-00 or 529-1011-00) / Organic Chemistry II (529-0222-00 or 529-1012-00). The number of participants is limited to 12.
551-1147-00L	Bioactive Natural Products from Bacteria Number of participants limited to 7. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	J. Piel
Abstract	Lab course. In small groups projects of relevance to current research questions in the field of bacterial natural product biosynthesis are addressed.
Learning objective	Introduction to relevant subjects of the secondary metabolism of bacteria. Training in practical work in a research laboratory. Scientific writing in form of a research report.
Content	Research project on bacteria that produce bioactive natural products (e.g., Streptomycetes, Cyanobacteria, uncultivated bacteria). The techniques used will depend on the project, e.g. PCR, cloning, natural product analysis, precursor feeding studies, enzyme expression and analysis.
Lecture notes	none.
Literature	Will be provided for each of the projects at the beginning of the course.
551-1554-00L	Multigene Expression in Mammalian Cells Number of participants limited to 5. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	P. Berger, G. Schertler
Abstract	Genetic engineering of mammalian cells with multiple expression cassettes is an essential need in contemporary cell biology. It is useful for protein expression for structural studies, the reprogramming of somatic cells, or for the expression of several fluorescently-tagged sensors. In this course, we use MultiLabel (Kriz et al., Nat. Commun., 2010) to create multigene expression plasmids.
Learning objective	Students will learn to design and clone multigene expression constructs for mammalian cells. The functionality of the constructs will be tested by immunofluorescence microscopy or Western blotting.
Content	We will clone fluorescently-tagged markers for subcellular compartments, assemble them to a multigene expression construct and transfect them into mammalian cells. These markers of subcellular compartments will be used to study the trafficking of activated receptors (e.g. serotonin receptor). Pictures will be taken on our microscopes and then we will quantify colocalization.
Lecture notes	none
551-0436-00L	Cryo-electron Microscopic Studies of Ribosomal Complexes with Biomedically Important Viral mRNAs Number of participants limited to 15. The enrolment is done by the D-BIOL study administration.	W	6 credits	7G	N. Ban, D. Böhringer, M. A. Leibundgut
Abstract	Some viral mRNAs, such as from Hepatitis C virus, hijack cellular translational machinery by binding directly to the ribosome and circumventing the need for cellular initiation factors. They accomplish this through structured elements within the mRNAs called internal ribosome entry sites (IRESs). Participants of this course will visualize ribosomes in complex with viral IRESs at high resolution.
Learning objective	The goal of the course is to acquire the most important techniques and methods for the purification and structural characterisation of macromolecular complexes by transmission electron microscopy. The emphasis of the course is on the special practical requirements for the application of these techniques on macromolecular structures in the MDa range.
Content	Protein synthesis is a very energy intensive process that can consume over half the total metabolism of a cell. In eukaryotes, translation is therefore tightly regulated at the stage of initiation. Regulatory processes are much more complex at this step than in prokaryotes and a large number of RNA modification processes and translation initiation factors are required to ensure faithful initiation, elongation and termination of translation. Viral messenger RNAs are often produced by their own machinery, however, and need to be incorporated into the host translation machinery without the usual processing and therefore many viruses have developed strategies to circumvent the need for initiation factors. They accomplish this through highly structured elements within their RNA called internal ribosome entry sites (IRESs) that are able to initiate translation without the normal signals. Some viral IRESs, such as the IRESs from polio-virus or HIV, require most of the normal eIFs and even additional proteins. Others, such as the hepatitis C virus IRES, are able to bind directly to the ribosome and need only a few of the normal initiation factors. Within the Ban lab, we have studied, and continue to investigate, medically relevant viral IRESs. The course will involve producing, and attempting to determine the structures of, IRESs that have yet to have had their ribosome-bound structures resolved. A variety of purification techniques, including preparative gel electrophoresis and ultracentrifugation, will be used during the purification of macromolecular complexes. Purified assemblies will be then investigated functionally. Students will then characterise their samples structurally through transmission electron cryo-microscopy (cryo-EM), including sample preparation, microscopy, data evaluation and the calculation of densities. Finally, students will learn how to build and refine molecular models into parts of the calculated cryo-EM density. The participants will be working on a closed project related to current research within the laboratory and throughout the course the practical work will be accompanied by brief theoretical introductions. The principal aim of the course is to strengthen the skills required to independently conduct meaningful biophysical and biochemical experiments and to provide an early introduction into the structural characterisation of cellular macromolecular assemblies.
Lecture notes	A script will be distributed at the beginning of the course that will cover the experiments to be performed, provide references to the relevant literature and suggest points for further consideration for interested students.
Literature	Literature A basic overview is provided within the references below. Further reading and citations shall be detailed in the course script. - A. Fersht, Structure and mechanism in protein science, Freeman, 1999 (Chapters 1 and 6). - M. van Heel et al., Single-particle electron cryo microscopy: towards atomic resolution, Quart. Rev. Biophys. (33), 307-369 (2000).
Prerequisites / Notice	The course will be held in English. Students should have either completed courses: 551-0307-00L Biomolecular Structure and Mechanism I: Protein Structure and Function 551-0307-01L Biomolecular Structure and Mechanism II: Large Cellular Machines or equivalent courses covering the structure and function of biological macromolecules.

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