Suchergebnis: Katalogdaten im Frühjahrssemester 2021

Nummer	Titel	Typ	ECTS	Umfang	Dozierende
Biologie Master
Wahlvertiefungen
Wahlvertiefung: Biologische Chemie
Obligatorische Konzeptkurse
529-0732-00L	Proteins and Lipids Hinweis für BSc Biologiestudierende: Nur einer der beiden Konzeptkurse 529-0731-00 Nucleic Acids and Carbohydrates (Herbstsemester) oder 529-0732-00 Proteins and Lipids (Frühlingsemester) kann für das Bachelorstudium angerechnet werden.	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, 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	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.
Lernziel	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.
Inhalt	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.
Skript	Printed lecture notes will be available for purchase at the beginning of the class. Problem sets and answer keys will be available on-line.
Literatur	No compulsory textbooks. Literature for further reading will be presented during the class and cited in the lecture notes.
Voraussetzungen / Besonderes	Course prerequisite: classes in organic and physical chemistry of the first two years of studies.
551-0224-00L	Advanced Proteomics Für Masterstudierende ab 2. Semester, Doktorierende und Postdoktorierende	W	4 KP	6G	P. Picotti, L. Gillet, 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	- 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 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 may 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: Molecular Machines and Cellular Assemblies 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 on advanced topics in Molecular Biology and Biochemistry will cover the structure and function of cellular assemblies. General topics in basic biochemistry will be further developed with examples of the function of large cellular machines involved in DNA packaging, translation, virus architecture, RNA processing, cell-cell interactions, and the molecular basis of CRISPER systems.
Lernziel	Students will gain a deep understanding of large cellular assemblies and the structure-function relationships governing their function in fundamental cellular processes. 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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