Prof. Dr. Sebastian Hiller

University of Basel
Klingelbergstrasse 50 / 70
CH - 4056 Basel
Biozentrum, Room 389 Phone: +41 61 207 20 82
Curriculum Vitae

Administrative Assistant

Jacqueline Staub
Biozentrum, Room 308
Phone: +41 61 207 21 01
Fax: +41 61 207 21 09


Anatole Abragam Prize for Prof. Björn Burmann

Björn Burmann, a former postdoc of Prof. Sebastian Hiller’s group at the...more

Cell Death: How a protein drives immune cells to suicide

For some pathogens, attack is the best form of defense - they enter immune...more

Immune cells on alert: Inflammasome activates emergency program

The inflammasome plays an important role in our body‘s immune defense. This...more

Research group Sebastian Hiller

Outer membrane proteins studied with NMR spectroscopy

Membrane proteins and their complexes fulfill biological key functions. We use nuclear magnetic resonance (NMR) spectroscopy to describe structural and functional details of integral outer membrane proteins and their biogenesis.

Structure of the mouse ASC inflammasome.

Proteins in the outer membranes of Gram-negative bacteria and mitochondria are responsible for a wide range of essential biological functions, including signal transduction, catalysis, respiration, and transport. We want to characterize the underlying molecular processes at atomic resolution by using NMR spectroscopy and related techniques. Part of our activities is the development of new and improved NMR techniques for membrane proteins and other challenging biomacromolecules.

Membrane-protein–chaperone complexes

As part of the biosynthesis of outer membranes of bacteria and mitochondria, chaperones are responsible for the transport of unfolded membrane proteins. We employ high-resolution NMR spectroscopy to provide a description of conformation and dynamics of large membrane-protein–chaperone complexes. We want to know the details how the protein transport is accomplished, how the substrates are recognized and how they are transferred between chaperones.

Outer membrane protein folding

As the last event in their biogenesis, outer membrane proteins are folded and inserted into the outer membrane by members of the Omp85 family of proteins. These are large protein machines which process their substrates in an energy-independent manner and thus function as foldases. We are currently attempting to unravel the folding and insertion mechanisms of the substrates and aim to characterize the intermediate steps of this process. We assume that the insertion mechanism includes the formation of a hybrid foldase-substrate barrel as the key intermediate event.

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 involved in cellular energy production, such as phosphate and nucleotides. The protein also has a major role in regulating metabolism and in programmed cell death, as well as in the development of cancer. In our latest experiments we are starting to understand the molecular prerequisites for these functions.