Our group is mainly focused on the development and application of NMR methodology for studying structure and function of biological macromolecules. We have contributed to the recent progress by designing sophisticated NMR methodology for the measurement of dihedral and orientational restraints in larger proteins, as well as by developing novel assignment strategies applicable for high molecular weight proteins.
Indeed, it is our goal, and even more so in the future, to make use of the methodological ingenuity to solve biological problems. Currently we are studying structure-function relationships of several proteins, including the ADF-H/cofilin family of proteins e.g. twinfilin, coactosin and cofilin, the glycoprotein chaperone ERp57, and the PrsA proteins from B. subtilis and S. aureus.
I work as a head for the National Biological NMR Center, which provides the state-of-the-art high-field NMR instrumentation, methodology and knowledge for the use of Finnish biological groups. My group has excellent equipment, software and knowledge for example to:
1) Solve protein's secondary and 3D structure
2) Study protein dynamics
3) Map ligand binding epitopes and determine dissociation constants
4) Determine 3D structures of ligand-protein complexes