Intrinsically disordered proteins (IDPs) or proteins containing intrinsically disordered regions (IDRs) are ubiquitous in eukaryotic proteome. In contrast to their structurally well-defined counterparts (i.e. folded proteins), IDPs typically lack persistent structure in their native form and do not necessarily require defined structure for molecular recognition and specific function. They are frequently involved in liquid-liquid phase separation (LLPS) driven assembly of various cellular condensates.
The main expertise of the group is centered on in vitro and in-cell single-molecule FRET spectroscopy, which is our main tool to look at IDPs and their interaction. For this purpose, we also use a variety of other state-of-the-art biochemical and biophysical techniques, such as biomolecular nuclear magnetic resonance (NMR) spectroscopy, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), live-cell imaging and others, to obtain a comprehensive picture of mechanisms of IDP interactions and to reveal the basis of specificity for molecular recognition and particular function of IDPs.
Currently, in the group we are working on the following research projects:
- investigation of eukaryotic translation initiation and especially the role of disordered translation initiation factors in this process;
- understanding the molecular mechanisms of function of disordered RNA-binding proteins in LLPS and cellular condensates;
- measuring biomolecular binding kinetics, including ternary complexes, fragile targets, strong non-specific binding, thanks to original methodological developments in SPR.