Collaborations

In collaborative studies, we employ microscope-based in vitro motility and single molecule mechanical assays to correlate the kinetic and spectroscopic properties of the motor constructs with their motile and mechanical parameters.


We investigate the structural basis the biochemical phenomena by various structural methods (crystallography, fiber X-ray diffraction, NMR spectroscopy, electron microscopy).



We also investigate the in vivo role of motor enzymes and their inhibition in the development of model organisms.
Methods and instrumentation used in our laboratory

Molecular biology, protein engineering, protein purification and modification

By mutagenesis and protein engineering, we create recombinant proteins for our studies using bacterial and eukaryotic (Dictyostelium and baculovirus-Sf9 insect cell) expression systems. In some cases, we apply subsequent site-specific modification of the proteins by means of protein chemistry.



Fluorescence spectroscopy

We apply a variety of steady-state and time-resolved fluorescence spectroscopic techniques to gain structural and dynamic information about the studied enzymes.




Enzyme kinetics

We investigate enzymatic mechanisms using steady-state and transient enzyme kinetic methods including rapid mixing (stopped-flow, quenched-flow) and kinetic relaxation (temperature-jump, flash photolysis) techniques.

   
 



In silico methods

We complement the experimental investigations by computational kinetic and structural modeling studies.


 
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