Invited Speakers

  Dr. Eckhard Bill

Max Planck Institute for Bioinorganic Chemistry, Mülheim an der Ruhr, Germany

  Dr. Bernadette Byrne

Imperial College London, UK

  Prof. Dr. Clemens Glaubitz

Goethe University, Frankfurt am Main, Germany

  Prof. Dr. Helmut Grubmüller

Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

  Prof. Dr. Eckhard Hofmann

Ruhr-Universität Bochum, Bochum, Germany

  Dr. Andrew Leslie

MRC Laboratory of Molecular Biology, Cambridge, UK

  Prof. Dr. Daniel Müller

ETH Zürich, Zürich, Switzerland

  Prof. Dr. Michael Sattler

Technical University Munich, Munich, Germany

  Prof. Dr. Ben Schuler

University of Zürich, Zürich, Switzerland

  Prof. Dr. Holger Stark

Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

Eckhard Bill is group leader at the Max Planck Institute for Bioinorganic Chemistry in Mülheim an der Ruhr. In his laboratory for ‘Molecular Paramagnetism and Bioinorganic Spectroscopy’ they combine 57Fe-Mössbauer spectroscopy, multi-frequency electron-paramagnetic-resonance spectroscopy (EPR), static magnetic susceptibility measurements, and magnetic circular-dichroism spectroscopy (MCD) for the study of bioinorganic compounds and metalloproteins. Low temperature measurements and magnetic fields (flux up to 7 and 10 Tesla) are regularly applied for the investigation of complex systems.

Bernadette Byrne is an expert in the production of membrane proteins for structural studies. Successes have included production, crystallisation and ultimately structure determination of the important respiratory enzymes: formate dehydrogenase-N and nitrate reductase-N from E. coli. More recent work in her group has focussed on the production of challenging membrane proteins including human G-protein coupled receptors and bacterial transporters. The inherent hydrophobic properties of these proteins has necessitated the development of novel methodologies, to deal with the key problem of non-specific aggregation of membrane protein at high concentrations.

Clemens Glaubitz is Professor at the Institute of Biophysical Chemistry and Managing Director of the Centre of Biomolecular Magnetic Resonance at the Goethe University in Frankfurt. Solid-state NMR spectroscopy is at the heart of the research projects of his group. They analyze the structure-function relationship of multidrug transport proteins directly within the lipid bilayer, investigate Proteorhodopsin in marine bacteria, look for structure and function of G protein-coupled receptors (GPCRs) and are interested in the mechanism by which GPCRs transfer information across the membrane.

Helmut Grubmüller is the managing director of the Max Planck Institute for Biophysical Chemistry in Göttingen, director of the Department of Theoretical and Computational Biophysics and Professor for Physics at the University of Göttingen. The theoretical biophysics group aims to contribute to the understanding of the physics and function of biomolecules - particularly proteins - at the atomic level. They wonder how a given protein work and how these structural and dynamical properties can be described in terms of many-body systems. New statistical mechanics concepts, quantum hybrid methods, and efficient parallel simulation algorithms and codes are the methodological focus of the department.

Eckhard Hofmann is head of the protein crystallography situated in the department of biophysics. The group is an integral part of the Protein Research Department at the Ruhr-University Bochum. To generate an atomic model of proteins and to generate a 3D- structure the group uses the method of X-ray protein crystallography. One focus of their work lies on proteins from the photosynthesis apparatus of algae and bacteria. Another area of interest is membrane proteins involved in active transport across the cytoplasmic membrane.

Andrew Leslie is group leader in the Division ‘Structural Studies’ at the MRC Laboratory of Molecular Biology in Cambridge, UK. He works on projects to determine the atomic structures of macromolecular complexes and membrane proteins using X-ray diffraction. His group aims to determine the structure of ATP synthase from mitochondria and is also working on integral membrane proteins, a wide variety of which perform crucial activities in living cells.

Daniel Müller holds the Chair of Biophysics at the ETH Zürich, Department of Biosystems Science and Engineering (D-BSSE). His research group develops bionanotechnological methods that allow high-resolution imaging (~ 1 nm) and quantifying inter- and intramolecular interactions of biological processes. Currently these methods allow to image proteins at work at (sub-)nanometer resolution, to quantify and localize cellular interactions at molecular resolution and to observe how individual receptors of living cells communicate.

Michael Sattler is Director of the Institute of Structural Biology at the Helmholtz Zentrum München, Neuherberg and Professor for Biomolecular NMR-Spectroscopy at the TU München. A main focus in the Sattler group is to understand the structural basis of protein-protein and protein-RNA interactions that are functionally important for various aspects of gene expression, such as the regulation of (alternative) pre-mRNA splicing and gene silencing by non-coding RNAs (siRNAs, miRNAs).

Ben Schuler is Professor for Biochemistry at the Biochemical Institute of the University Zürich. In his research projects he investigates the folding, misfolding, and dynamics of proteins in a multidisciplinary approach, using a close combination of biochemical and biophysical methods, in particular single molecule fluorescence spectroscopy. Especially in combination with Förster resonance energy transfer (FRET), the intrinsically heterogeneous processes of both folding and misfolding of proteins are tested by quantifying structural distributions, their dynamics, and the underlying molecular mechanisms.

Holger Stark is leader of the BioFuture group at the Max-Planck-Institute for Biophysical Chemistry in Göttingen. The work in his group is focused on 3D structure determination of large macromolecular complexes by single particle electron cryomicroscopy (cryo-EM). The major research interest concentrates on macromolecular complexes related to pre-mRNA splicing, translation and cell cycle regulation and on the development of new methods to improve sample preparation, imaging and computational image processing techniques.