Our group works mostly on methodological aspects of NMR spectroscopy. The aim of this work is faster and more accurate determination of structurally important NMR parameters, and their application in chemistry and biochemistry. Recently we focus on the development of new approaches for acquisition of multidimensional NMR spectra necessary in the studies of biomolecules. Most important topics include: development of new pulse sequences for faster or more accurate determination of spectral parameters, methods of fast acquisition of multidimensional spectra, determination of scalar and residual dipolar couplings, chiral recognition.
Currently our work focuses on the following tasks:
- Acquisition of high dimensional NMR spectra (4-7D) and new strategies of resonance assignment in biomolecules.
- Application of new methods for the studies of intrinsically disordered proteins (IDP).
- Development of methods for cleaning spectra from artefacts which are result of sparse sampling. This would allow analysis of spectra featuring high dynamic range of peak amplitudes, as for example heteronuclear edited 4D NOESY.
- Development of NMR methods exploring the new possibilities of random sampling for the accurate and precise determination of scalar and residual dipolar couplings from 3 and 4D NMR spectra.
- Protein structure elucidation and protein interaction studies.
- Peptide structure elucidation.
