Resolution in a new dimension for solving challenges of society

1.2 GHz at the Max-Planck Institute for Biophysical Chemistry in Göttingen

High field GHz-Class Magnets used for finding solutions for Structural Biology key questions

A key principle in biology is: structure determines function. Our customers try to understand how molecules interact with each other and then modify their function.

This is key in finding solutions against diseases like: Alzheimer, Parkinson, Cancer and covid-19.
The increased spectral resolution and sensitivity of the 1.2 GHz NMR has already enabled research teams to look more deeply at proteins and better understand the initial steps of amyloid-type protein aggregation as well as the function and structure of the Tau protein, both commonly associated with Alzheimer’s disease.

1.2 GHz at the Max-Planck Institute for Biophysical Chemistry in Göttingen

Research includes the structures, dynamics and function of important globular proteins, membrane proteins and protein complexes.

Ultra-high field NMR is also unique in that it can study the properties and interactions of intrinsically disordered proteins (IDPs), which make up 30-50% of the human proteome. IDPs play a crucial functional rule in fundamental cell biology, and they are also implicated in many instances of disease biology.

Prof. Dr. Christian Griesinger and Prof. Dr. Markus Zweckstetter gave us an interesting insight about their work with the new 1.2 GHz How do molecules behave under disease conditions? How can we use this knowledge to find cures for disease like Alzheimer and Parkinson.

1.2 GHz at the ETH Zürich

The Bio-NMR group, headed by Roland Riek, is part of the Laboratory of Physical Chemistry at the Department of Chemistry and Applied Biosciences of the Swiss Federal Institute of Technology (ETH) Zurich.

Nuclear Magnetic Resonance Spectroscopy (NMR) is one of the principal experimental techniques in structural biology to determine atomic resolution structures and to investigate dynamic features and intermolecular interactions of biological macromolecules. Using NMR as a major tool, the objective of the research in our group is to understand the conformational switches of proteins associated with amyloid diseases and trans-membrane signaling.

Prof. Dr. Roland Riek, is part of the Laboratory of Physical Chemistry at the Department of Chemistry and Applied Biosciences of the Swiss Federal Institute of Technology (ETH) Zurich.

1.2 GHz at the University Düsseldorf/ Forschungszentrum Jühlich

The function of each cell and each organism decisively depends on the dynamic interactions between biological macromolecules and on their correct three-dimensional structure. Faulty interaction and incorrectly folded structures eventually lead to diseases and ageing.

The aim of the Institute for Physical Biology at the Heinrich Heine University of Düsseldorf is to understand these interactions and to determine the three-dimensional structure of the protein complexes involved in decisive cellular processes - if possible, in atomic resolution.

They are interested in understanding the structural features of life's key players and to use their insights to identify new therapeutic opportunities to interfere with disease-related processes.

In this respect the Etzkorn Group at the Institute for Physical Biology of the Heinrich Heine University Düsseldorf focuses on the following topics:

Membrane systems in neuronal signalling, NMR method development, Biocatalysis.

Dr. Manuel Etzkorn is Heisenberg group leader at the Institute of Physical Biology at the Heinrich Heine University Düsseldorf, Germany