Zurich — Researchers at the University of Zurich (UZH) are using a new, high-performance nuclear magnetic resonance spectrometer to analyse complex biomolecular structures. The goal is to gain insights through basic research in molecular biology for the benefit of medicine or the development of new pharmaceutical compounds.
(CONNECT) Researchers at the University of Zurich (UZH) are using a new nuclear magnetic resonance (NMR) spectrometer, installed in November 2025, to analyze complex biomolecular structures. According to a press release, the team of scientists led by Oliver Zerbe intends to analyse these structures in order to gain insights for both basic biochemical research and medicine and pharmacology.
According to the operating principle of a nuclear magnetic resonance spectrometer, the spins of atoms such as carbon or hydrogen align in a magnetic field. If radio waves are directed at such a sample—for example, organic molecules suspended in a liquid—their echoes can be measured as an NMR spectrum. The larger these molecules are, the more complex the spectrum is. For research purposes, this means building an NMR spectrometer with a high resonance frequency in order to detect all signals reflected by the sample separately. This is possible with the new facility at UZH, which can generate a magnetic field strength of 25.8 tesla. “The resolution of this spectrometer is simply much higher than that of previous devices—similar to a larger camera sensor,” Oliver Zerbe, co-leader of the NMR team, is quoted as saying in the press release. "This allows us, for example, to better understand how substances bind to large, complex molecules in bacterial cells."
Zerbe's team is currently investigating the antibacterial effects of the naturally occurring protein thanatin. Insights from NMR spectroscopy are expected to offer ways to modify thanatin so that it prevents the formation of bacterial protective coats. Another area of research is the structural characterisation of intrinsically disordered proteins (IDPs), which do not have a fixed structure but consist largely of flexible chains. Among other things, IDPs act as signal transmitters during cell division. A prominent example of an IDP is the p53 molecule, which has been studied worldwide and, under normal conditions, prevents cells with damaged genetic material from dividing.
The 1.2-gigahertz NMR spectrometer is one of three such instruments currently available to researchers in Europe. The cost of 13.5 million Swiss francs is shared by UZH, the Swiss Federal Institute of Technology Zurich (ETH), and the University of Basel under a joint usage agreement (Swiss High-field NMR Facility). ce/ww
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