Research Groups

Group Allain

Prof. Frederic Allain

Almost 20% of genetic diseases originate from a post-transcriptionnal misregulation of gene expression that is often correlated with errors in pre-mRNA alternative splicing and/or RNA editing. The knowledge of parameters involved in these misregulations at the molecular level can help understanding these diseases and finding out new ways of treatment.

Group Ban

Prof. Nenad Ban

Structural and functional studies of ribosomes and other supramolecular assemblies
The main goal of the research in my laboratory is to study structures of prokaryotic and eukaryotic ribosomes, ribosomal subunits and their complexes with various factors involved in protein synthesis with an aim to better understand this process. Recently, we have expanded our studies to investigate structure and function of large eukaryotic multienzyme complexes such as the fatty acid synthase, a giant multifunctional enzyme that contains seven catalytic domains and catalyses all steps of fatty acid synthesis. We are using crystallography as the primary method in combination with electron microscopy and biochemical experiments.

Group Berger

PD Dr. Imre Berger

An intense focus of current biological research efforts is the elucidation of protein interaction networks (interactome). Many large multiprotein complexes are discovered. This poses considerable challenges for molecular level studies, in particular for eukaryotic multiprotein complexes with intracellular quantities refractory to large-scale extraction from source. Our research is focused on developing new technologies to obtain, within a reasonable time-frame, well-defined and homogeneous samples of human multiprotein assemblies in transcription and hereditary disease, which we then use for high-resolution structural and functional analyses.

Group Glockshuber

Prof. Rudi Glockshuber

Protein folding and assembly

The three-dimensional structure of a protein is exclusively determined by its amino acid sequence and is formed in an autonomous and spontaneous process. Compared to protein folding in vitro, the kinetics and the yields of folding in the living cell are significantly increased by enzymes catalyzing rate-limiting folding steps or preventing nonproductive folding reactions. We are trying to answer general questions on protein folding with particular focus on the mechanism and structural biology of catalyzed disulfide bond formation and the assembly of adhesive type 1 pili in bacteria. 

Group Locher

Prof. Kaspar Locher

Structure and mechanism of membrane transport proteins

Transport of nutrients and waste products across membranes is essential to cellular life. We explore, at a molecular level, how integral membrane proteins transport substrates across the lipid bilayer. Our main focus is on ATP-binding cassette (ABC) transporters, a large family of proteins that couple unidirectional substrate transport to the hydrolysis of ATP. Human ABC proteins are associated with various diseases including cystic fibrosis or multi-drug resistance of cancer cells, whereas bacterial homologs mediate nutrient uptake and drug extrusion. We determine the structures of ABC transporters at high resolution using X-ray crystallography and we study their dynamics and in vitro transport kinetics after reconstitution in liposomes.

Group Richmond

Prof. Tim Richmond

The group's research focuses is on the X-ray crystallographic structures of the nucleosome core particle and the chromatosome, two sub-elements of the nucleosome, as well as crystal structures of several transcription factor protein/DNA complexes. These factors include members of the basic domain, leucine zipper family, the human serum response factor, and basal factor complexes. The stability of these assemblies is also under investigation by thermodynamic and kinetic means to complement our structural studies. Our goal is to provide an atomic resolution, molecular picture for gene regulation in higher organisms.

Group Weber-Ban

Prof. Eilika Weber-Ban

We are interested in structure-function studies of multi-subunit macromolecular assemblies and their mechanistic and allosteric properties. The current focus of interest is the bacterial ClpAP multisubunit protease. Its function is the ATP-dependent disaggregation and degradation of proteins. The analysis of the functional and mechanistic role of a member of this family can make important contributions to the more general understanding of the role of these proteins in pro- and eukaryotic cells and their potential involvement in abnormal cellular function.

Group Wider

Prof. Gerhard Wider

Based on new structure determinations of biologically interesting macromolecules we improve existing and develop new NMR experiments. Further, for proteins with known X-ray structure we develop new assignment methods that also work for large molecules where conventional techniques fail. We are interested in aqueous as well as in nonaqueous solutions. In the latter enzymes cannot only be active but also exhibit intriguing new properties, however, the phenomenon is not yet understood in detail since there are very limited structural and dynamic data at atomic resolution.

Group Wüthrich

Prof. Kurt Wüthrich

Development of NMR Methodology for Studies of Biological Macromolecules, NMR solution studies of the E. coli GroEL/GroES system, NMR Structure Determination of the Prion Protein, Automation of NMR Spectral Analysis and Protein Structure Determination, biophysical and structural investigation of the prion protein, and others are the main interests of our research.

Group Ishikawa

Dr. Takashi Ishikawa (Dept. of Biology)

We are studying ATP-driven motor proteins, especially dynein and FoF1 ATP synthase from Chlamydomonas, using three-dimensional cryo-electron microscopy. The mechanism to convert tiny (5-10 Å) structural changes of motor proteins caused by ATP hydrolysis into huge linear, rotational or bending motions (~100 Å) are still to be investigated. To explore the range of motion of motor proteins in complex with their partners, structures of each individual (not averaged) particles (a molecule or a complex of molecules) must be visualized at sufficiently high resolution. We develop the methodology that fulfills these demands, combining two methods of 3D cryo-electron microscopy: single particle analysis and electron tomography, in order to visualize the structure of motor proteins and their complexes during dynamic motions under the condition close to in vivo.