CRC 1093 - Practical Courses

Integrated Graduate School – Practical Courses Supramolecular Chemistry and Biology

All Graduate Students within the CRC have the chance to participate in practical training courses or scientific work in another laboratory, in order to learn new experimental methods or techniques.

It is recommended that the graduate students do the practical course or the lab exchange program within the first two years of their PhD work so that they can benefit from them for their own experimental studies. The successful participation will be certificated.

Below the information about the different practical courses are listed. PhD students can choose among the following:

A1 Schmuck Solid phase synthesis

High-throughout screening of combinatorial libraries, synthesis and screening of dynamic combinatorial libraries

When: In semester breaks by agreement; No. of participants: 3

A2 Kaiser Proteomics

Chemical synthesis of bioreactive probes, chemical proteomics (including sample preparation, in vitro/vivo labeling, mass spectrometry).

When: In semester breaks by agreement; No. of participants: 3

A3 Schrader Biophysical affinity determination

ITC, fluorescens titrations.

When: In semester breaks by agreement; No. of participants: 3

A5 Epple Synthesis and characterization of inorganic nanoparticles, loaded with biomolecules

Dynamic light scattering, disc centrifugal sedimentation, scanning electron microscopy.

When: Twice every year in March and in October; further courses if sufficiently high demand;

Duration: 1 week;  No. of participants: 3

A6 Saccà DNA origami structures

Design of simple planar DNA origami; self-assambly of DNA origami; AFM characterization.

When: On previous agreement; No. of participants: 4

A7 Hoffmann Bioinformatics methods, statistical methods, biomolecular modeling methods

Students are guided in the solution of problems from their respective projects using computational methods

When: In semester breaks by agreement; No. of participants: 2

A8 Sanchez QM/MM and MD methods for the study of biomolecules

Molecular dynamics simulations, enhanced sampling approaches and multi-scale methods, among others.

When: In semester breaks by agreement; No. of participants: 3

A9 Schlücker Raman spectroscopy

Spectroscopic techniques such as UV/Vis extinction and surface-enhanced Raman spectroscopy (SERS).

When: according to prior agreement; No. of participants: 6

A10 Voskuhl Synthesis and characterisation of novel luminophores with aggregation induced emission properties

Measurement of fluorescence and absorption spectra as well as quantum efficiencies.

When: according to prior agreement; No. of participants: max. 2

A11 Hartmann Precision macromolecules and polymers

Solid phase synthesis of peptides and Oligo(amidoamines), analytics of Ligand-Receptor-Interaction with surface plasmon resonance (SPR), Analytics and purification of macromolecules with HPLC and GPC.

When: according to prior agreement; No. of participants: max. 2

B1 Ehrmann Complex assembly & changes in oligomeric state of a protein complex following chemical denaturation and refolding

PCR cloning, expression, protein purification and enzyme assays.

When: In semester breaks by agreement; No. of participants: 3

B2 Meyer Protein interaction studies in mammalian tissue culture cells

Cloning of mammalian expression constructs; Transfection, coIP, gel filtration, western blot analysis.

When: In semester breaks by agreement; No. of participants: 3

B4 Ottmann Biophysical analysis of protein-protein interactions

Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC) and a number of plate-reader based methods (FP, HTRF, AlphaScreen) to analyze Protein-Protein Interactions.

When: In semester breaks by agreement; No. of participants: 3

B5 Knauer Microinjection and (confocal) fluorescence microscopy

Handling of a conventional fluorescence microscope; Microinjection of recombinant proteins into living cells, monitored by live cell imaging; Basic confocal microscopy.

When: In semester breaks by agreement; No. of participants: 3

B6 Musacchio Protein expression in prokaryotic and eukaryotic hosts - a primer on protein purification techniques

Recombinant protein expression in bacterial and insect cell hosts; Methods of macromolecular purification, including affinity, ion exchange, and size-exclusion chromatography and basic biochemical techniques.

When: In semester breaks by agreement; No. of participants: 3

B7 Westermann Primer on genetic manipulation and analysis of the budding yeast Saccharomyces cerevisiae - a classic eukaryotic model organism

Design of integration constructs, generation of knock-out alleles and creation of fusion proteins. Strategies for analysis of growth phenotypes, protein-protein interactions and cell cycle progression.

When: In semester breaks by agreement; No. of participants: 2

Z2 Vetter Macromolecular X-Ray structure analysis

 

When: In semester breaks by agreement; No. of participants: 3

Z3 Bayer Protein-NMR

 

When: In semester breaks by agreement; No. of participants: 3

Overview about CRC1093 practical courses

Description and Organisation of Crc1093-practical-courses