Suchergebnis: Katalogdaten im Frühjahrssemester 2018

Biologie Master Information
Wahlvertiefungen
Wahlvertiefung: Biologische Chemie
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, 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, 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.
SkriptCourse material from the individual lecturers wil be made available at the sharepoint website

Link
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 Link
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
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.
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 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.
LernzielInsight 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.
InhaltPart 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
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.
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