Teaching
The following table gives an overview of lectures and practical classes that are offered to each member of the Leibniz Graduate School. The courses are organized in blocks of single or consecutive days in order to decrease the commute times within Berlin. Each course comprises lectures and practical courses and amounts to 4 SWS. Two classes within the first 2 years are mandatory for each scholar.
Overview
Block Course | Lecturer | Location |
Quantum Chemistry and EPR Methods | Bittl/Alexiev | FU |
Ultrafast dynamics and microscopic interactions | Elsässer | MBI |
Purification, Characterization and Crystalization of Membrane Proteins | Hegemann | HU |
Protein Crystallography and methods for X-ray structure refinement | Heinemann | MDC |
Membrane Biophysics and Fluorescence Microscopy | Herrmann | HU |
Biophysical Investigations of Signal Transduction Processes | Hofmann | Charite |
Electrophysiological investigation of mutated ion channel proteins | Jentsch | FMP |
Thermodynamic Approaches to Membrane Proteins | Keller | FMP |
Solution-state NMR methods and restrained molecular dynamics | Oschkinat | FMP |
NMR Spectroscopy of Biomolecules | Reif | FMP |
Molekulare Pharmakologie und zelluläre Signaltransduktion | Rosenthal | FMP |
Thermodynamics and kinetics of protein folding and ligand binding | Seckler | U Potsdam |
Methods in Electron-Microscopy | Spahn | Charité |
Coherent laser spectroscopy | Wöste / Siebert | FU |
Nuclear magnetic resonance (NMR) spectroscopy of small biomolecules: Hyperpolarization and relaxation" | Vieth | FU |
Topics
Quantum Chemistry and EPR Methods
Membranbiophysik
Date
SS 2007; SWS: 4.0; 2std.V+2std.Ü/Praktikum
Vorlesung und Praktikum/Übungen (9:00 - 18:00 Uhr)
Time
Blockkurs: 23. - 27. Juli 2007
(ab 10 Teilnehmern bis 03.08.07)
Vorbesprechung:
Mo 07. Mai, 16:00 Uhr
Organiser
Dr. Ulrike Alexiev
Freie Universität Berlin
Institut für Experimentalphysik I
Arnimallee 14
13195 Berlin
Tel.: 030 / 838 55157
Email: alexiev(at)physik.fu-berlin.de
Abstract
Aufbau von Biomembranen, physikalische Grundlagen ihrer Organisation, Transportprozesse entlang und über Membranen, Elektrostatik an der Membran/Wasser Grenzfläche, Membranproteine und ihre Interaktion mit der Membran, physikalische Methoden zur Charakterisierung der Membranen (experimentelle Methoden und MD-Simulationen).
Link: http://www.physik.fu-berlin.de
Thermodynamic Approaches to Membrane Proteins
Date: 15th–19th September 2008
Organiser
Dr. Sandro Keller
Biophysics of Membrane Proteins
Leibniz Institute of Molecular Pharmacology FMP
Robert-Rössle-Str. 10
13125 Berlin
+49 30 9406 3064 (tel)
+49 30 9406 3065 (fax)
email: keller'at'fmp-berlin.de
Number of participants
3–5
Objectives
- Understanding the thermodynamic principles underlying the insertion of membrane proteins into lipid bilayers and their folding and oligomerisation within the hydrophobic membrane environment.
- Familiarising with the preparation and handling of samples containing hydrophobic peptides and proteins as well as membrane-mimetic systems such as artificial lipid vesicles and detergent micelles.
- Applying spectroscopic (UV absorption, fluorescence, and circular dichroism) and calorimetric (isothermal titration, differential scanning, and pressure perturbation calorimetry) methods to characterise membrane proteins.
Lectures
- Thermodynamics of bilayer insertion, folding, and oligomerisation of membrane proteins.
- Spectroscopic and microcalorimetric methods for studying membrane proteins.
Practical courses
- Handling of membrane proteins, lipid vesicles, and detergent micelles
- Isothermal titration calorimetry (ITC)
- Differential scanning calorimetry (DSC)
- Pressure perturbation calorimetry (PPC)
- UV absorption spectroscopy
- Fluorescence spectroscopy
- Circular dichroism (CD) spectroscopy
Measuring Transbilayer Lipid Movement and Membrane Fusion
Date
May 27 - 30, 2008
Unit responsible for teaching the subject
Prof. Dr. Thomas Pomorski, Prof. Dr. Andreas Herrmann
Humboldt Universität zu Berlin
Mathematisch-Naturwissenschaftliche Fakultät I
Institut für Biologie/Biophysik
Invalidenstrasse 42
D-10115 Berlin
Tel.: 49-30-2093-8860
Fax : 49-30-2093-8585
email: andreas.herrmann'at'rz.hu-berlin.de
Number of participants
2–3
Objectives of theoretical part of teaching in this subject
Introduction into Membrane Fusion (Lecture); Introduction into Transbilayer Lipid Dynamics (Lecture); Paper Discussion/Presentation on Fluorescence Techniques and Single Molecule Detection.
Objectives of practical part of teaching in this subject
Course I Virus Fusion analyzed by Fluorescence Spectroscopy); Course II Virus Fusion analyzed by Fluorescence Microscopy); Course III Transbilayer Lipid Movement analyzed by Fluorescence Spectroscopy); Course IV Intracellular lipid transport analyzed by Thin layer chromatography). You will perform experiments in all courses.
Course material/presentation
You will receive a scripte describing the background and experiments in detail. The lectures are based on powerpoint presentation including videos; you will have to prepare presentation for the paper discussion.
Prerequisites for taking this subject
Strong commitment to membrane biology and biophysical techniques.
Electrophysiological investigation of mutated ion channel proteins
Date
2007 July 23 – August 3 (first week part-time, then full day)
Place
FMP/MDC, Timofeyev-Ressovky-Haus (Genomhaus), 2 floor
Number of participants
up to 3 participants
Organiser
Prof. Dr. Thomas Jentsch
Leibniz-Insitut für Molekulare Pharmakologie (FMP) and Max-Delbrück-Centrum für Molekulare Medizin (MDC)
Robert-Rössle-Str. 10
13125 Berlin
Tel.: +49(30)9406-2961
email: jentsch'at'fmp-berlin.de
How to sign up
If interested, please contact me by email until 15th of June 2007.
Abstract
The practical course intends to confer basic theoretical and experimental understanding of structure-function analysis of ion channel proteins by site-directed mutagenesis. The techniques involved include basic molecular biology, preparation and injection of Xenopus oocytes, and investigations of expressed currents using two-electrode-voltage clamping.
A channel cDNA will be mutated by PCR using mutagenesis primers, cloning of the new expression construct and preparation of plasmid DNA, in vitro RNA transcription, preparation and injection of frog oocytes with this RNA, and finally voltage-clamping of oocytes. As several incubation times are needed (e.g. growing of transformed bacterial, incubation of oocytes), not all days of the practical course will require full-day attendance. <//font><//font>
Biophysics of Signal Transduction
Date
2007
May 22-25
May 29-June 1
June 5-8
(all day) 4SWS
Place
Institute of Medical Physics and Biophysics
Ziegelstr. 5-9
Berlin
Number of participants
18
How to sign up
Condition for the participation at this course is the previous participation at the lecture "Biophysics of Signal Transduction" by Prof. K. P. Hofmann (SS 2007).
Abstract
The aim of this course is to impart basic knowledge on various spectroscopic techniques such as UV/ Vis- FTIR- and VCD (Vibrational Circular Dichroism) spectroscopy. The course comprises three different experiments: In the FTIR experiment the task is to determine the secondary structure of selected proteins and their thermal stability by analysis of the amide I band. VCD spectroscopy is applied to quantitatively determine the content of the (+) and (-) enantiomers in a solution of a terpenoid compound containing both isomers. In the third experiment intermediates of the photoreceptor rhodopsin will be investigated by UV/ Vis spectroscopy. The pKa for the transition from the inactive Meta I intermediate to the active Meta II intermediate shall be determined.
Nuclear magnetic resonance (NMR) spectroscopy of biomolecules: Basic principles and applications
Date
2008 October 13-24 (all day), 4 SWS
Place
FMP Berlin, ground floor, small seminar room
Organiser
Prof. Dr. Bernd Reif
Leibniz-Insitut für Molekulare Pharmakologie (FMP)
Robert-Rössle-Str. 10
13125 Berlin
Tel.: 030 / 94793-191
email: reif'at'fmp-berlin.de
Number of participants
up to 5 participants
How to sign up
If interested, please contact me by email until 15th of June 2007.
Abstract
The practical course intends to mediate a basic understanding of theory and applications of solution-state and solid-state NMR spectroscopy, as well as magnetic resonance imaging (MRI).
The programm is split into two parts, covering the theoretical aspects of NMR spectroscopy in lectures in the mornings. Practical aspects including spectral assignments, determination of constitution and conformation of small molecules, peptides and proteins are covered in the afternoons.
The teaching programm covers the fundamental principles in quantum mechanics, introduction of the product operator formalism, Fourier-Transform (FT) NMR spectroscopy, basic aspects of relaxation theory, nuclear Overhauser enhancement (nOe) spectroscopy, 2D and 3D NMR spectroscopy, magic angle spinning (MAS) solid-state NMR, structural analysis of oriented membrane proteins, structure determination of biomolecules in solution- and in the solid-state.
Femtosecond laser spectroscopy: Control of photo-induced molecular processes via tailored, ultrashort laser pulses
Date
03. – 14. September, 2007 (all day), 4 SWS
Place
Physics Institute, FU-Berlin, seminar room 1.4.39.
Organiser
Prof. Dr. L. Wöste / Dr. T. Siebert
Institut für Experimentalphysik
Freie Universität Berlin
14195 Berlin
Tel.: 030 / 838-56122
email: woeste'at'physik.fu-berlin.de
email: siebert'at'physik.fu-berlin.de
Number of participants
up to 5 participants
How to sign up
Please contact by email until 31. July, 2007.
Abstract
The course will present the general concepts of femtosecond spectroscopy and its application to the observation and control of ultrafast molecular dynamics. The curriculum includes the generation, amplification and spectral broadening of ultrashort laser pulses as well as the construction of complex pulse forms with spatial light modulators in framework of coherent control of photo-induced molecular processes.
The two week program will be divided into two sections. In the first week, the generation of ultrashort laser pulses will be treated, including lectures on the working principle of femtosecond oscillators and amplifiers (lasing, Kerr-lens mode-locking, chirped pulse amplification and spectral broadening via self-phase modulation) accompanied by a "hands on" laboratory course in the operation of a femtosecond laser system (tuning and adjustment of a femtosecond oscillator as well as the variation and characterization of its output). The second week will present the fundamental principles of time-resolved spectroscopy of ultrafast molecular processes and the coherent control of molecular dynamics (pump-probe spectroscopy, Tannor-Rice and Brummer-Shapiro control strategies as well as the optimal control scheme developed by H. Rabitz). The lectures in this week will be accompanied with a laboratory course in the shaping of ultrashort laser pulses (spatial light modulators) and their characterization (frequency resolved optical gating - FROG).
Purification, Characterization and Crystalization of Membrane Proteins
Date
Sommersemester 2008
24.06. - 04.07.2008
Vorbesprechung
09.06. 2008, 12.00 Uhr
Ort: Invalidenstr. 42, 3. Etage
Organiser
Prof. Peter Hegemann
Humboldt-Universität Berlin
Institut für Experimentelle Biophysik
Invalidenstr. 42
Berlin 10115
Tel.: 030/ 2093 8681
email: hegemape'at'rz.hu-berlin.de
How to sign up
Please contact the organizer by email.
Abstract:
Charakterisierung und Kristallisation von Membranproteinen (Bakteriorhodopsin), Isolierung von Bacteriorhodopsin (BR) aus Halobakterien, Analyse der einzelnen Reinigungsfraktionen mittlels Absorptionsspektroskopie und SDS-Page
Charakterisierung von Wildtyp BR und der langsamen Mutante D96N, reversible Bleichung, Transportaktivität, Bioenergetik, Blitzlichtphotolyse, Solubilisierung des BR in Detergenz, Reinigung, Kristallisation, Charakterisierung der verschiedenen Kristallisationsbedingungen.
Molekulare Pharmakologie und zelluläre Signaltransduktion
Time
Wochentag der Vorlesung: Mittwoch
Uhrzeit: 17.30 Uhr – 19.00 Uhr
Places
Hörsaal, Institut für Pharmakologie, CBF, Thielallee 67, 14195 Berlin
Organiser
Prof. Dr. Ricardo Hermosilla
PD Dr. Alexander Oksche
Institut für Pharmakologie, CBF
Thielallee 67-73
14195 Berlin
email: ricardo.hermosilla'at'charite.de
email: alexander.oksche'at'charite.de
Vorlesung
G-Protein-gekoppelte Rezeptoren
Effektorsysteme von G-Protein-gekoppelten Rezeptoren
Protein-Struktur-Analysen mittels NMR
Neurotransmitterfreisetzung und Vesikel-recycling
Calciumhomöostase
Stammzellen
Transgene Techniken
Signaltransduktion des Sehens
Nukleäre Steroidrezeptoren
Zelladhäsionsmoleküle
Mechanorezeption
A-Kinase Ankerproteine
Wnt-Signalweg
Seminar
Wochentag(e) des Seminars: jeden 2. Mittwoch
Uhrzeit: 19.15 Uhr – 20.00 Uhr
Veranstaltungsort: Hörsaal, Institut für Pharmakologie, CBF, Thielallee 67, 14195 Berlin
Abstract
Die fachbereichsübergreifende Lehrveranstaltung Wahlfach “Molekulare Pharmakologie“ soll Studenten die Gelegenheit geben, sich mit derzeit relevanten Fragen und Methoden der molekularen Pharmakologie, Schwerpunkt zelluläre Signaltransduktion, auseinanderzusetzen.
Protein Crystallography and methods for X-ray structure refinement
Titles
Introduction into Protein Crystallography, lecture
Protein Structure Analysis, practical course (up to 12 participants)
Special Topics of Protein Crystallography, lecture
Structure Analysis of Biological Macromolecules, seminar
Date
2008 June 02 - 20 (all day), 21 SWS
Places
Institut für Chemie und Biochemie, FU Berlin, Takustr. 6, SR 3. floor (weeks 1 and 2)
MDC Berlin, SR 0211 (week 3)
BESSY GmbH, Albert-Einstein-Str. 15, 12489 Berlin (week 4, optional)
Organiser
Prof. Dr. Udo Heinemann
Max-Delbrück-Centrum für Molekulare Medizin Berlin-Buch (MDC)
Robert-Rössle-Str. 10
13125 Berlin
Tel.: 030 / 9406-3420
email: heinemann'at'mdc-berlin.de<//font>
How to sign up
If interested, please contact me by email until 30th of May 2008.
Abstract
This course is taught by Drs. Wolfram Sanger (FU Berlin), Udo Heinemann (MDC Berlin) and Uwe Müller (BESSY, Berlin). The 2 lectures, the seminar and the laboratory course are one unit. The fourth week is optional (but it is also the highlight that one should not miss). Therefore, the time commitment must be 3 weeks all day (without highlight) or 4 weeks all day (with highlight).
The course aims at getting students acquainted with macromolecular crystallography. At the end of the course, students will have know enough to start a diploma or masters work in a laboratory using macromolecular crystallography as an experimental technique. Those who choose other career paths will know enough basics to use and critically assess the results of crystallographic analyses for their own work in any area of the life sciences.
The program covers all aspects of macromolecular crystallography. The theory of protein crystallization, crystal symmetry, X-ray diffraction, phasing, electron density generation, model fitting, refinement and validation are taught in the lectures and practiced in the seminar. Hands-on experience in all these things is gained. Weeks 1 and 2 are mainly on proteins, week 3 is on nucleic acids, and week 4 is on the use of synchrotron radiation anomalous diffraction in crystallography<//font>
Nuclear magnetic resonance (NMR) spectroscopy of biomolecules: Basic principles and applications (2008)
Date
February 2009, 2 weeks
Places
FMP Berlin, ground floor, small seminar room
Number of participants
up to 5 participants
Organiser
Prof. Dr. Hartmut Oschkinat
Leibniz-Insitut für Molekulare Pharmakologie (FMP)
Robert-Rössle-Str. 10
13125 Berlin
Tel.: 030 / 94793-161
email: oschkinat'at'fmp-berlin.de
How to sign up
If interested, please contact me via email.
Abstract
The course introduces into the basics of solution-state NMR spectroscopy of biomacromolecules. Practical aspects (set-up of experiments on spectrometer, assignment of multidimensional NMR spectra), as well as theoretical aspects are covered in lectures and practicals.
