Suchergebnis: Katalogdaten im Frühjahrssemester 2019

Nummer	Titel	Typ	ECTS	Umfang	Dozierende
Biologie Master
Wahlvertiefungen
Wahlvertiefung: Molekular- und Strukturbiologie
Wahlpflicht Konzeptkurse Siehe D-BIOL Master-Wegleitung
551-0314-00L	Microbiology (Part II)	W	3 KP	2V	W.‑D. Hardt, L. Eberl, H.‑M. Fischer, J. Piel, J. Vorholt-Zambelli
Kurzbeschreibung	Advanced lecture class providing a broad overview on bacterial cell structure, genetics, metabolism, symbiosis and pathogenesis.
Lernziel	This concept class will be based on common concepts and introduce to the enormous diversity among bacteria and archaea. It will cover the current research on bacterial cell structure, genetics, metabolism, symbiosis and pathogenesis.
Inhalt	Advanced class covering the state of the research in bacterial cell structure, genetics, metabolism, symbiosis and pathogenesis.
Skript	Updated handouts will be provided during the class.
Literatur	Current literature references will be provided during the lectures.
Voraussetzungen / Besonderes	English
551-0324-00L	Systems Biology	W	6 KP	4V	R. Aebersold, B. Christen, M. Claassen, U. Sauer
Kurzbeschreibung	Introduction to experimental and computational methods of systems biology. By using baker’s yeast as a thread through the series, we focus on global methods for analysis of and interference with biological functions. Illustrative applications to other organisms will highlight medical and biotechnological aspects.
Lernziel	- obtain an overview of global analytical methods - obtain an overview of computational methods in systems biology - understand the concepts of systems biology
Inhalt	Overview of global analytical methods (e.g. DNA arrays, proteomics, metabolomics, fluxes etc), global interference methods (siRNA, mutant libraries, synthetic lethality etc.) and imaging methods. Introduction to mass spectrometry and proteomics. Concepts of metabolism in microbes and higher cells. Systems biology of developmental processes. Concepts of mathematical modeling and applications of computational systems biology.
Skript	no script
Literatur	The course is not taught by a particular book, but some books are suggested for further reading: - Systems biology in Practice by Klipp, Herwig, Kowald, Wierling und Lehrach. Wiley-VCH 2005

Wahlpflicht Masterkurse
Nummer	Titel	Typ	ECTS	Umfang	Dozierende
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 KP	2V	R. Glockshuber, T. Ishikawa, S. Jonas, B. Schuler, D. Veprintsev, E. Weber-Ban
Kurzbeschreibung	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.
Lernziel	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".
Inhalt	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.
Skript	Course material from the individual lecturers wil be made available at the sharepoint website https://team.biol.ethz.ch/e-learn/551-1402-00L
Voraussetzungen / Besonderes	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.
551-0224-00L	Advanced Proteomics Für Masterstudierende ab 2. Semester, Doktorierende und Postdoktorierende	W	4 KP	6G	R. Aebersold, L. Gillet, M. Gstaiger, A. Leitner, P. Pedrioli
Kurzbeschreibung	Ziel dieses Kurses ist es, etablierte und neue Technologien der Protein- und Proteome-Analyse kennenzulernen in Bezug auf ihre Anwendung in Biologie, Biotechnologie und Medizin. Format: Einführung durch Dozent mit anschliessender Diskussion, unterstützt durch Literaturarbeit und Übungen.
Lernziel	Im Kurs werden sowohl die bereits etablierten als auch die neuesten derzeit entstehenden Technologien und Methoden in der Protein- und Proteomanlayse diskutiert im Hinblick auf ihre Anwendung in der Biologie, Biotechnologie, Medizin und Systembiologie.
Inhalt	Block course teaching current methods for the acquisition and processing of proteomic datasets.
Voraussetzungen / Besonderes	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
551-0364-00L	Functional Genomics Information for UZH students: Enrolment to this course unit only possible at ETH. No enrolment to module BIO 254 at UZH. Please mind the ETH enrolment deadlines for UZH students: Link	W	3 KP	2V	C. von Mering, C. Beyer, B. Bodenmiller, M. Gstaiger, H. Rehrauer, R. Schlapbach, K. Shimizu, N. Zamboni, weitere Dozierende
Kurzbeschreibung	Functional genomics is key to understanding the dynamic aspects of genome function and regulation. Functional genomics approaches use the wealth of data produced by large-scale DNA sequencing, gene expression profiling, proteomics and metabolomics. Today functional genomics is becoming increasingly important for the generation and interpretation of quantitative biological data.
Lernziel	Functional genomics is key to understanding the dynamic aspects of genome function and regulation. Functional genomics approaches use the wealth of data produced by large-scale DNA sequencing, gene expression profiling, proteomics and metabolomics. Today functional genomics is becoming increasingly important for the generation and interpretation of quantitative biological data. Such data provide the basis for systems biology efforts to elucidate the structure, dynamics and regulation of cellular networks.
Inhalt	The curriculum of the Functional Genomics course emphasizes an in depth understanding of new technology platforms for modern genomics and advanced genetics, including the application of functional genomics approaches such as advanced microarrays, proteomics, metabolomics, clustering and classification. Students will learn quality controls and standards (benchmarking) that apply to the generation of quantitative data and will be able to analyze and interpret these data. The training obtained in the Functional Genomics course will be immediately applicable to experimental research and design of systems biology projects.
Voraussetzungen / Besonderes	The Functional Genomics course will be taught in English.
551-1100-00L	Infectious Agents: From Molecular Biology to Disease Number of participants limited to 22. Requires application until 2 weeks before the start of the semester; selected applicants will be notified one week before the first week of lectures. (if you missed the deadline, please come to the first date to see, if there are any slots left)	W	4 KP	2S	W.‑D. Hardt, L. Eberl, U. F. Greber, A. B. Hehl, M. Kopf, S. R. Leibundgut, C. Münz, A. Oxenius, P. Sander
Kurzbeschreibung	Literature seminar for students at the masters level and PhD students. Introduction to the current research topics in infectious diseases; Introduction to key pathogens which are studied as model organisms in this field; Overview over key research groups in the field of infectious diseases in Zürich.
Lernziel	Working with the current research literature. Getting to know the key pathogens serving as model organisms and the research technologies currently used in infection biology.
Inhalt	for each model pathogen (or key technology): 1. introduction to the pathogen 2. Discussion of one current research paper. The paper will be provided by the respective supervisor. He/she will give advice (if required) and guide the respective literature discussion.
Skript	Teachers will provide the research papers to be discussed. Students will prepare handouts for the rest of the group for their assigned seminar.
Literatur	Teachers will provide the research papers to be discussed.
Voraussetzungen / Besonderes	Restricted to max 22 students. Please sign up until two weeks before the beginning of the semester via e-mail to micro_secr@micro.biol.ethz.ch and include the following information: 551-1100-00L; your name, your e-mail address, university/eth, students (specialization, semester), PhD students (research group, member of a PhD program? which program?). The 22 students admitted to this seminar will be selected and informed by e-mail in the week befor the beginning of the semester by W.-D. Hardt. The first seminar date will serve to form groups of students and assign a paper to each group.
551-1404-00L	RNA and Proteins: Post-Transcriptional Regulation of Gene Expression (University of Zurich) Der Kurs muss direkt an der UZH belegt werden. UZH Modulkürzel: BCH252 Beachten Sie die Einschreibungstermine an der UZH: https://www.uzh.ch/cmsssl/de/studies/application/mobilitaet.html	W	3 KP	2V	Uni-Dozierende
Kurzbeschreibung	The course introduces the cellular processes and molecular mechanisms involved in regulating genome expression at the post-transcriptional level. Topics will include : -RNA processing, and transport; -protein synthesis and translational control, trafficking and degradation; -RNA-guided regulation (RNA interference, microRNAs); -molecular surveillance and quality control mechanisms
Lernziel	-Outline the cellular processes used by eukaryotic and prokaryotic cells to control gene expression at the post- transcriptional level. -Describe the molecular mechanisms underlying post-transcriptional gene regulation -Identify experimental approaches used to study post-transcriptional gene regulation and describe their strengths and weaknesses.
551-1412-00L	Molecular and Structural Biology IV: Visualizing Macromolecules by X-Ray Crystallography and EM	W	4 KP	2V	N. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, weitere Dozierende
Kurzbeschreibung	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.
Lernziel	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.
Inhalt	February 22 Lecture 1 Prof. Dr. Kurt Wüthrich History of Structural Molecular Biology March 1 Lecture 2 Prof. Dr. Kaspar Locher X-ray diffraction from macromolecular crystals March 8 Lecture 3 Prof. Dr. Kaspar Locher Data collection and statistics, phasing methods March 15 Lecture 4 Prof. Dr. Nenad Ban Crystal symmetry and space groups March 22 Lecture 5 Ban Lab Practical session with X-ray data processing March 29 Lecture 6 Prof. Dr. Takashi Ishikawa 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) April 5 Lecture 7 Dr. Daniel Boehringer Single particle analysis, including principle (projection matching, random conical tilt, angular reconstitution) April 12 Lecture 8 Ban Lab Practical session including specimen preparation (cryo, negative stain, visit to ScopeM May 3 Lecture 9 Prof. Dr. M. Pilhofer Tomography I, including basics and subtomogram averaging May 10 Lecture 10 Ban Lab Practical session with example initial EM data processing May 17 Lecture 11 Prof. Dr. Martin Pilhofer Practical session (including recent techniques, including cryo-FIB) May 24 Lecture 12 Prof. Dr. Nenad Ban EM and X-ray structure building, refinement, validation and interpretation May 31 Lecture 13 Ban Lab Practical session with model building and refinemen
551-1414-00L	Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR	W	4 KP	2V	F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
Kurzbeschreibung	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.
Lernziel	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.
Inhalt	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
Literatur	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.

Wahlvertiefung: Biologische Chemie
Obligatorische Konzeptkurse
Nummer	Titel	Typ	ECTS	Umfang	Dozierende
529-0732-00L	Proteins and Lipids	O	6 KP	3G	D. Hilvert
Kurzbeschreibung	An overview of the relationship between protein sequence, conformation and function.
Lernziel	Overview of the relationship between protein sequence, conformation and function.
Inhalt	Proteins, structures and properties, (bio)synthesis of polypeptides, protein folding and design, protein engineering, chemical modification of proteins, proteomics.
Literatur	General Literature: - T.E. Creighton: Proteins: Structures and Molecular Properties, 2nd Edition, H.W. Freeman and Company, New York, 1993. - C. Branden, J. Tooze , Introduction to Protein Structure, Garland Publishing, New York, 1991. - J. M. Berg, J. L. Tymoczko, L. Stryer: Biochemistry, 5th edition, H.W. Freeman and Company, New York, 2002. - G.A. Petsko, D. Ringe: Protein Structure and Function, New Science Press Ltd., London, 2004. Original Literature: Citations from the original literature relevant to the individual lectures will be assigned weekly.

Wahlpflicht Masterkurse
Nummer	Titel	Typ	ECTS	Umfang	Dozierende
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 KP	2V	R. Glockshuber, T. Ishikawa, S. Jonas, B. Schuler, D. Veprintsev, E. Weber-Ban
Kurzbeschreibung	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.
Lernziel	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".
Inhalt	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.
Skript	Course material from the individual lecturers wil be made available at the sharepoint website https://team.biol.ethz.ch/e-learn/551-1402-00L
Voraussetzungen / Besonderes	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 KP	3G	D. Opris
Kurzbeschreibung	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.
Lernziel	Understanding the significance of molecular size, constitution, configuration and conformation of synthetic and natural macromolecules for their specific physical and chemical properties.
Inhalt	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.
Skript	Course materials (consisting of personal notes and distributed paper copies) are sufficient for exam preparation.
Voraussetzungen / Besonderes	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 KP	3G	Y. Yamakoshi, B. M. Lewandowski
Kurzbeschreibung	Prinzipien molekularer Erkennung: Komplexierung von Anionen, Kationen und technol. Anwendungen; Kompl. von Neutralmolekülen in wässr. Lösung; nichtkovalente Wechselwirkungen mit aromatischen Ringen; Wasserstoffbrückenbindungen; molekulare Selbstassoziation – ein chemischer Zugang zu Nanostrukturen; Thermodynamik und Kinetik von Komplexierungsprozessen; Synthese von Rezeptoren; Templateffekte.
Lernziel	Ziel der Vorlesung ist das Verständnis von Natur und Stärke der nichtkovalenten zwischenmolekularen Wechselwirkungen sowie von Solvatationseffekten bei der Assoziation von Molekülen und/oder Ionen. Die Vorlesung (2 h) wird durch eine Übungsstunde (1 h) ergänzt, bei der die Synthese von Rezeptoren und andere synthetische Aspekte der Supramolekularen Chemie im Vordergrund stehen.
Inhalt	Prinzipien molekularer Erkennung: Komplexierung von Kationen und Anionen sowie entspr. technologische Anwendungen, Komplexierung von Neutralmolekülen in wässriger Lösung, nichtkovalente Wechselwirkungen mit aromatischen Ringen, Wasserstoffbrückenbindungen, Selbstassoziation von Molekülen – ein chemischer Zugang zu Nanostrukturen, Thermodynamik und Kinetik von Komplexierungsprozessen; Synthese von Rezeptoren; Templateffekte.
Skript	Ein Skript kann zu Beginn der Vorlesung erworben werden. Übungsaufgaben und Lösungen werden über das Internet zur Verfügung gestellt.
Literatur	Keine Pflichtliteratur. Ergänzungsliteratur wird im Rahmen der Vorlesung und im Skript vorgestellt.
Voraussetzungen / Besonderes	Voraussetzungen: organisch- und physikalisch-chemische Vorlesungen der ersten zwei Studienjahre.
551-0224-00L	Advanced Proteomics Für Masterstudierende ab 2. Semester, Doktorierende und Postdoktorierende	W	4 KP	6G	R. Aebersold, L. Gillet, M. Gstaiger, A. Leitner, P. Pedrioli
Kurzbeschreibung	Ziel dieses Kurses ist es, etablierte und neue Technologien der Protein- und Proteome-Analyse kennenzulernen in Bezug auf ihre Anwendung in Biologie, Biotechnologie und Medizin. Format: Einführung durch Dozent mit anschliessender Diskussion, unterstützt durch Literaturarbeit und Übungen.
Lernziel	Im Kurs werden sowohl die bereits etablierten als auch die neuesten derzeit entstehenden Technologien und Methoden in der Protein- und Proteomanlayse diskutiert im Hinblick auf ihre Anwendung in der Biologie, Biotechnologie, Medizin und Systembiologie.
Inhalt	Block course teaching current methods for the acquisition and processing of proteomic datasets.
Voraussetzungen / Besonderes	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 KP	2V	N. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, weitere Dozierende
Kurzbeschreibung	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.
Lernziel	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.
Inhalt	February 22 Lecture 1 Prof. Dr. Kurt Wüthrich History of Structural Molecular Biology March 1 Lecture 2 Prof. Dr. Kaspar Locher X-ray diffraction from macromolecular crystals March 8 Lecture 3 Prof. Dr. Kaspar Locher Data collection and statistics, phasing methods March 15 Lecture 4 Prof. Dr. Nenad Ban Crystal symmetry and space groups March 22 Lecture 5 Ban Lab Practical session with X-ray data processing March 29 Lecture 6 Prof. Dr. Takashi Ishikawa 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) April 5 Lecture 7 Dr. Daniel Boehringer Single particle analysis, including principle (projection matching, random conical tilt, angular reconstitution) April 12 Lecture 8 Ban Lab Practical session including specimen preparation (cryo, negative stain, visit to ScopeM May 3 Lecture 9 Prof. Dr. M. Pilhofer Tomography I, including basics and subtomogram averaging May 10 Lecture 10 Ban Lab Practical session with example initial EM data processing May 17 Lecture 11 Prof. Dr. Martin Pilhofer Practical session (including recent techniques, including cryo-FIB) May 24 Lecture 12 Prof. Dr. Nenad Ban EM and X-ray structure building, refinement, validation and interpretation May 31 Lecture 13 Ban Lab Practical session with model building and refinemen
551-1414-00L	Molecular and Structural Biology V: Studying Macromolecules by NMR and EPR	W	4 KP	2V	F. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
Kurzbeschreibung	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.
Lernziel	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.
Inhalt	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
Literatur	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.

Zusätzliche Konzeptkurse
Nummer	Titel	Typ	ECTS	Umfang	Dozierende
551-0320-00L	Cellular Biochemistry (Part II)	W	3 KP	2V	Y. Barral, R. Kroschewski, A. E. Smith
Kurzbeschreibung	This course will focus on molecular mechanisms and concepts underlying cellular biochemistry, providing advanced insights into the structural and functional details of individual cell components, and the complex regulation of their interactions. Particular emphasis will be on the spatial and temporal integration of different molecules and signaling pathways into global cellular processes.
Lernziel	The full-year course (551-0319-00 & 551-0320-00) focuses on the molecular mechanisms and concepts underlying the biochemistry of cellular physiology, investigating how these processes are integrated to carry out highly coordinated cellular functions. The molecular characterization of complex cellular functions requires a combination of approaches such as biochemistry, but also cell biology and genetics. This course is therefore the occasion to discuss these techniques and their integration in modern cellular biochemistry. The students will be able to describe the structural and functional details of individual cell components, and the spatial and temporal regulation of their interactions. In particular, they will learn to explain how different molecules and signaling pathways can be integrated during complex and highly dynamic cellular processes such as intracellular transport, cytoskeletal rearrangements, cell motility, and cell division. In addition, they will be able to illustrate the relevance of particular signaling pathways for cellular pathologies such as cancer or during cellular infection.
Inhalt	Spatial and temporal integration of different molecules and signaling pathways into global cellular processes, such as cell division, cell infection and cell motility. Emphasis is also put on the understanding of pathologies associated with defective cell physiology, such as cancer or during cellular infection.
Literatur	Recommended supplementary literature (review articles and selected primary literature) will be provided during the course.
Voraussetzungen / Besonderes	To attend this course the students must have a solid basic knowledge in chemistry, biochemistry, cell biology and general biology. Biology students have in general already attended the first part of the "Cellular Biochemistry" concept course (551-0319-00). The course will be taught in English. In addition, the course will be based on a blended-learning scenario, where frontal lectures will be complemented with carefully chosen web-based teaching elements that students access through the ETH Moodle platform.
551-0307-01L	Molecular and Structural Biology II: From Gene to Protein D-BIOL students are obliged to take part I and part II as a two-semester course.	W	3 KP	2V	N. Ban, F. Allain, S. Jonas, M. Pilhofer
Kurzbeschreibung	This course will cover advanced topics in molecular biology and biochemistry with emphasis on the structure and function of cellular assemblies involved in expression and maintenance of genetic information. We will cover the architecture and the function of molecules involved in DNA replication, transcription, translation, nucleic acid packaging in viruses, RNA processing, and CRISPER/CAS system.
Lernziel	Students will gain a deep understanding of large cellular assemblies and the structure-function relationships governing their function in fundamental cellular processes ranging from DNA replication, transcription and translation. 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.
Inhalt	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.
Skript	Updated handouts will be provided during the class.
Literatur	The lecture will be based on the latest literature. Additional suggested literature: Branden, C., and J. Tooze, Introduction to Protein Structure, 2nd ed. (1995). Garland, New York.

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