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Atomic structures of proteins elucidated


The more we know about the agents that cause disease, the more specifically we will be able to combat them. These are the words of Prof. Adam Lange of the Leibniz-Institut für Molekulare Pharmakologie Berlin (FMP) looking back over his work of the past five to ten years. Lange and his Department of Molecular Biophysics have developed new solid-state NMR methods (nuclear magnetic resonance spectroscopy) for elucidation of the atomic structure of proteins. With these methods, the researchers for the first time determined structures of proteins that are involved in various infection processes and thus contributed to a molecular understanding of bacterial infection.

For his newly developed methods applied to bacterial proteins, Adam Lange has now been awarded the Founders' Medal at the International Conference of Magnetic Resonance in Biological Systems (ICMRBS) in Kyoto, Japan. The prize, to which the amount of 3,000 US dollars is attached, is one of the most important accolades in the field of NMR spectroscopy and was awarded to the 39-year old biophysicist on 23 August during the six-day conference. "This award recognizes your major contributions to the development and application of solid-state NMR to biological systems," declared the Chair of the selection committee, Prof. Mei Hong of the Massachusetts Institute of Technology (MIT).. Meanwhile, Lange explained that he was accepting the award on behalf of his team. "This prize is the reward for many years of constructive teamwork," he said in Kyoto.

The award is not in recognition of one single piece of work, but the systematic development of methods over the past years. At the same time, the NMR-based determination of protein structures has already led to spectacular individual discoveries: For example, Lange and his team have for the first time elucidated the structure of the bacterial injection needle of the type III secretion system in atomic resolution. Bacteria such as salmonellae or the EHEC pathogens use these needles to inject molecular agents into their host cells. A further milestone was the elucidation of the atomic structure of bactofilin - an important element of the bacterial cytoskeleton, which was only recently discovered. Bactofilin, for example, gives Helicobacter bacteria the screw shape that enables them to bore into the gastric mucosa, where they can cause inflammations and ulcers.

"We are conducting basic research here," says Lange, "but against the backdrop of the growing number of antibiotic resistances, we are driven by the idea of finding new approaches to the treatment of infections, such as novel anti-infectives that have a more specific effect and act much earlier than traditional antibiotics."

Adam Lange moved from the Max Planck Institute for Biophysical Chemistry in Göttingen to the Leibniz-Institut für Molekulare Pharmakologie in Berlin in 2014. Since then, he has headed the Department of Molecular Biophysics there; parallel to this, he is teaching "The structure and dynamics of biomolecules" at the Humboldt University of Berlin as part of a W3-S professorship.

The structural biologist has managed to secure large amounts of third-party funding for his work at the FMP. For example, he initially received an Emmy Noether grant from the Deutsche Forschungsgemeinschaft (DFG); at present, he is being funded with a grant from the European Research Council (ERC).

Source: Leibniz-Institut für Molekulare Pharmakologie (FMP)