What we study
The central theme is the relationship between the spatial structure and function of membrane and membrane-active proteins and their interactions with ligands. Much of the work is applied: oncology, neurodegenerative disease, pain mechanisms, diagnostics.
Main topics
Membrane proteins and receptors
Transmembrane domains of receptor tyrosine kinases, toll-like receptors, GPCRs; homo- and heterodimerisation of transmembrane helices as a signalling mechanism.
Ion channels
Sodium and potassium channels: the structural basis of conduction and its modulation by ligands and toxins.
Amyloid precursor protein (APP)
Structure and interactions of APP; disruption of transmembrane-domain dimerisation as a factor in Alzheimer's disease.
Neurotoxins
Toxins from snake, insect and spider venoms as modulators of ion channels and receptors, and as molecular tools.
Antimicrobial and membrane-active peptides
Channel-forming peptides and their mechanisms — e.g. transmembrane β-hairpin dimers as the basis of antimicrobial activity.
Plant defence peptides and lipid-transfer proteins
Hevein-like peptides and their interaction with chitin, lipid-transfer proteins, protease inhibitors.
Methods & facilities
The work relies on an integrated methodology for structural-dynamic studies, combining NMR and EPR spectroscopy, protein engineering and computational modelling.
The laboratory operates three Bruker Avance spectrometers at 600, 700 and 800 MHz with cryogenic probes; one instrument enables solid-state NMR with magic-angle spinning. In-house systems for bacterial and cell-free synthesis of recombinant proteins and for isotope-labelled samples (¹⁵N, ¹³C, ²H), as well as membrane-mimicking media, support the full cycle of sample preparation.
Methodological developments include pulse sequences for heteronuclear measurements and software for biomolecular relaxation-data analysis (the DASHA program). The laboratory is part of the IBCh RAS shared-use research centre.