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.
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.
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.