Protein structure, function and dynamics
Team leader: dr Rafał Augustyniak
Team leader’s e-mail address: rafal.augustyniak@uw.edu.pl
Brief description of the research topic:
The Protein structure, function and dynamics group focuses on investigating the relationship between structure, dynamics, and function of proteins under near-physiological conditions. The primary experimental technique employed in these studies is solution NMR spectroscopy, supported by complementary biochemical and spectroscopic methods. The group has expertise in advanced isotope labeling strategies and methyl group spectroscopy, enabling the analysis of large and complex protein systems (ranging from over 50 kDa up to 1 MDa).
An integral part of the group’s activities involves using molecular biology techniques to design and produce recombinant proteins, which are then subjected to detailed biophysical characterization. The available infrastructure includes UV-Vis spectroscopy, fluorescence- based techniques, and light scattering. In collaboration with external partners, additional imaging-based approaches such as fluorescence microscopy, DLS (dynamic light scattering), and FRAP (fluorescence recovery after photobleaching) are also employed.
The group studies globular proteins and intrinsically disordered proteins or regions (IDPs/IDRs), focusing on their ability to form condensed assemblies through liquid–liquid phase separation (LLPS). The aim is to understand how structural features, post-translational modifications, and interactions with molecular partners modulate the biological activity of these systems.
Ongoing research projects include:
(1) the HP1α protein – investigating the role of phosphorylation and metal ion binding in regulating chromatin condensation (currently funded by the NCN),
(2) the MeCP2 protein – exploring its potential regulation via interactions with proline-rich domain-binding proteins (in collaboration with Dr. Alaji Bah, Upstate University),
(3) the transcription factor IRF7 – a key regulator of immune response,
(4) the translation initiation factor eIF5B – focusing on its intrinsically disordered N-terminal region (in collaboration with Prof. Michael Marr, Brandeis University).
The group applies an interdisciplinary approach combining advanced biophysical and spectroscopic techniques with modern molecular biology methods to study protein function in its native biological context.