Welcome!
Our research aims at understanding the
structure and functional mechanisms of biological membranes and
membrane proteins at an atomic level. Despite the central importance of
membranes in providing functional boundaries for cells, current
knowledge on membrane proteins is limited. This is mainly due to
challenges in obtaining samples suitable for use with conventional
experimental methods.

We employ recently developed techniques of
nuclear magnetic resonance (NMR) spectroscopy to solve some of these
problems. In particular, we are interested in elucidating the
structural basis for mechanisms of membrane biogenesis and transport by
studying proteins from the membrane insertion and translocation
machinery of gram-negative bacteria and mitochondria. Important
components of our work in this area are the expression, purification
and reconstitution of membrane proteins, as well as the application and
further development of solution state NMR techniques.
In addition, we aim to extend the applicability
of NMR by developing methods for the use of hyperpolarization. Such
pre-polarization of nuclear spins can yield signal enhancements of up
to 10,000 fold when compared to conventional NMR. Dynamic nuclear
polarization (DNP) is a newly available hyperpolarization technology,
which we use to explore specific processes such as ligand binding both
at equilibrium and transiently. This is of particular importance to
investigate, for example, mechanisms of signaling, as well as to
develop new applications for determining ligand binding in drug
discovery.