Suchergebnis: Katalogdaten im Frühjahrssemester 2019

Biologie Master Information
Wahlvertiefungen
Wahlvertiefung: Biologische Chemie
Obligatorische Konzeptkurse
NummerTitelTypECTSUmfangDozierende
529-0732-00LProteins and LipidsO6 KP3GD. Hilvert
KurzbeschreibungAn overview of the relationship between protein sequence, conformation and function.
LernzielOverview of the relationship between protein sequence, conformation and function.
InhaltProteins, structures and properties, (bio)synthesis of polypeptides, protein folding and design, protein engineering, chemical modification of proteins, proteomics.
LiteraturGeneral 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
NummerTitelTypECTSUmfangDozierende
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 KP2VR. Glockshuber, T. Ishikawa, S. Jonas, B. Schuler, D. Veprintsev, E. Weber-Ban
KurzbeschreibungThe 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.
LernzielThe 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".
InhaltThe 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.
SkriptCourse material from the individual lecturers wil be made available at the sharepoint website

https://team.biol.ethz.ch/e-learn/551-1402-00L
Voraussetzungen / BesonderesFinished 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 KP3GD. Opris
KurzbeschreibungBasic 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.
LernzielUnderstanding the significance of molecular size, constitution, configuration and conformation of synthetic and natural macromolecules for their specific physical and chemical properties.
InhaltThis 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.
SkriptCourse materials (consisting of personal notes and distributed paper copies) are sufficient for exam preparation.
Voraussetzungen / BesonderesThe 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 KP3GY. Yamakoshi, B. M. Lewandowski
KurzbeschreibungPrinzipien 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.
LernzielZiel 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.
InhaltPrinzipien 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.
SkriptEin Skript kann zu Beginn der Vorlesung erworben werden. Übungsaufgaben und Lösungen werden über das Internet zur Verfügung gestellt.
LiteraturKeine Pflichtliteratur. Ergänzungsliteratur wird im Rahmen der Vorlesung und im Skript vorgestellt.
Voraussetzungen / BesonderesVoraussetzungen: organisch- und physikalisch-chemische Vorlesungen der ersten zwei Studienjahre.
551-0224-00LAdvanced Proteomics Belegung eingeschränkt - Details anzeigen
Für Masterstudierende ab 2. Semester, Doktorierende und Postdoktorierende
W4 KP6GR. Aebersold, L. Gillet, M. Gstaiger, A. Leitner, P. Pedrioli
KurzbeschreibungZiel 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.
LernzielIm 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.
InhaltBlock course teaching current methods for the acquisition and processing of proteomic datasets.
Voraussetzungen / BesonderesNumber 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
551-1412-00LMolecular and Structural Biology IV: Visualizing Macromolecules by X-Ray Crystallography and EMW4 KP2VN. Ban, D. Böhringer, T. Ishikawa, M. A. Leibundgut, K. Locher, M. Pilhofer, K. Wüthrich, weitere Dozierende
KurzbeschreibungThis 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.
LernzielStudents 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.
InhaltFebruary 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
551-1414-00LMolecular and Structural Biology V: Studying Macromolecules by NMR and EPRW4 KP2VF. Allain, A. D. Gossert, G. Jeschke, K. Wüthrich
KurzbeschreibungThe 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.
LernzielInsight 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.
InhaltPart 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
Literatur1) 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
NummerTitelTypECTSUmfangDozierende
551-0320-00LCellular Biochemistry (Part II)W3 KP2VY. Barral, R. Kroschewski, A. E. Smith
KurzbeschreibungThis 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.
LernzielThe 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.
InhaltSpatial 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.
LiteraturRecommended supplementary literature (review articles and selected primary literature) will be provided during the course.
Voraussetzungen / BesonderesTo 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.
551-0307-01LMolecular 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.
W3 KP2VN. Ban, F. Allain, S. Jonas, M. Pilhofer
KurzbeschreibungThis 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.
LernzielStudents 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.
InhaltAdvanced class covering the state of the research in structural molecular biology of basic cellular processes with emphasis on the function of large cellular assemblies.
SkriptUpdated handouts will be provided during the class.
LiteraturThe 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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