16 September 2026
Leonardo Levorin from the Institute of Biological Information Processing - Structural Biochemistry (IBI-7) at Forschungszentrum Jülich has been awarded the 2026 Ernst Prize by the Division of Magnetic Resonance of the German Chemical Society (GDCh). The award recognises a scientific publication in which Levorin and his colleagues used nuclear magnetic resonance (NMR) measurements to gain new insights into protein folding and dynamics.
Proteins are not rigid structures. They move, fold and, depending on their environment, can adopt different shapes. A single structural 'snapshot' is therefore often not enough to fully understand how they function. The research team therefore investigated entire ensembles of possible protein conformations.
To do this, the researchers used solid-state NMR spectroscopy. The technique uses strong magnetic fields to examine how certain atomic nuclei behave within a molecule. Their signals can provide information about the structure and mobility of a protein. In this particular application of solid-state NMR, the proteins are studied in frozen solution. The different conformations present at the moment of freezing are thus preserved and leave characteristic signatures in the NMR spectrum.
The award-winning work focused on the amino acid isoleucine. Its side chain acts, in a sense, as a molecular reporter of motion: its signals reveal how much conformational freedom individual regions of a protein have. Levorin and the research team were able to show that the mobility of the side chains is closely linked to the structural rigidity of the respective protein region.
The results also illustrate that not all 'unfolded' states are alike. Even proteins without a fixed three-dimensional structure can adopt a very wide range of conformations, depending on the environmental conditions. This knowledge helps researchers better understand the processes involved in protein folding and misfolding. Such processes play an important role in neurodegenerative diseases, among other conditions.
As part of the study, Levorin carried out extensive solution- and solid-state NMR measurements, combining a range of methods. These included DNP-enhanced solid-state NMR. This technique can substantially enhance the inherently weak NMR signals, allowing them to be measured more accurately. In this work, he benefited from the excellent infrastructure of the Biomolecular NMR Centre at Forschungszentrum Jülich, which is operated at IBI-7 in cooperation with Heinrich Heine University Düsseldorf.
The award ceremony took place on 15 September 2026 as part of the 47th Annual Discussion Meeting of the GDCh Division of Magnetic Resonance in Mainz. Leonardo Levorin presented his award-winning research in a lecture at the meeting.
The work demonstrates that understanding proteins requires looking not only at their shape, but also at their mobility and the many different states they can adopt.
Award for early-career researchers
The Ernst Prize honours the memory of Nobel Laureate in Chemistry Richard R. Ernst, who made seminal contributions to the development and application of magnetic resonance. The GDCh Division of Magnetic Resonance awards up to three Ernst Prizes each year to students and doctoral researchers for an outstanding original scientific publication.
Original publication:
Leonardo Levorin et al.: *Isoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR.* Journal of the American Chemical Society (2025). DOI: 10.1021/jacs.5c04159
Contact Persons
Leonardo Levorin
PhD Student
- Institute of Biological Information Processing (IBI)
- Structural Biochemistry (IBI-7)
