J. Heyrovsky Institute of Physical Chemistry of the Academy of Sciences of the Czech Republic

The impact of transmembrane domains on the organisation of membrane proteins
Cellular membranes are composed of a large number of lipid species. Similarly, membrane proteins own transmembrane domains (TMDs) which are well conserved for protein isoforms or between species but highly dissimilar between individual proteins. We are studying the impact of TMDs on the organisation of proteins in cellular membranes. More, we are addressing this issue also by investigation peptides derived from the TMDs in model membranes using fluorescence techniques.
Structure-localisation-function axis of CD4 and CD8 co-receptors in T cells
In is now well established there is strong correlation between localisation and function of proteins in cells. We are interested which sturctural motifs of CD4 and CD8 co-receptors in T cells define their unique function in T cells. More, nanoscopic localisation is always determined and correlation between protein surface distribution and function investigated.
Single molecule localisation microscopy and other fluorescence techniques to study cellular membranes
Home-built single molecule fluorescence microscope was built in our laboratory with help of Ales Benda and Peter Kapusta. We are employing fluorescence techniques including PALM, SOFI, FRET, FCS and solvent relaxation to investigate behaviour of molecules in model and cellular membranes. This can happen due to a tight collaboration with members of Fluorescence Group of Prof. Martin Hof at our department (see the link below).
Hof Fluorescence Group