Research group Sebastian Hiller

Membrane proteins studied with nuclear magnetic resonance (NMR) spectroscopy

Most membrane proteins have important biological functions and are therefore also often of great medical significance. By using nuclear magnetic resonance spectroscopy, we aim at understanding structure, function, and folding of membrane proteins and their complexes.

Three-dimensional structure of the VDAC membrane protein.

Membrane proteins assume important tasks within the cells of all forms of life, such as signaling or the transport of biomolecules. We want to understand these processes better and are using nuclear magnetic resonance (NMR) spectroscopy to study membrane proteins at atomic resolution. We focus on selected membrane protein systems of high biological and medical significance, in particular from the membranes of mitochondria, the "powerhouses" of the cell.

The VDAC membrane protein

One example of our work is the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane. VDAC allows the passage of molecules important for cell energy, such as phosphate and nucleotides, and has a major role in regulating metabolism and in programmed cell death (apoptosis), as well as in the development of cancer. In our latest experiments we are now starting to understand the molecular prerequisites for these functions. Further interesting systems are subject to our research.

New NMR techniques

Parallel to working on biological questions, we develop and improve advanced NMR techniques. Our aim is to progressively increase the number of protein systems to which NMR is applicable. We are developing new methods of data collection and processing, automated spectroscopy and new approaches to isotope labeling and preparation of membrane proteins.