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Helmholtz Munich I Daniela Barreto

New method to investigate the structure and dynamics of challenging membrane proteins

Featured Publication, Molecular Targets and Therapeutics, STB,

Researchers created a new approach to reduce the complexity of the NMR experiments and facilitate the investigation of membrane protein systems of pharmaceutical importance.

In a new study, the team led by Prof. Franz Hagn, scientist at the Helmholtz Munich Institute of Structural Biology, used so-called split-inteins to produce membrane proteins that are only partially visible in nuclear magnetic resonance (NMR) spectroscopy experiments. NMR spectroscopy is a versatile method for the investigation of the structure, dynamics and interactions of (bio-)molecules, such as proteins, at high resolution but is limited by severe signal overlap with large biomolecules. The reported approach markedly reduces the complexity of the NMR measurements and heavily facilitates the investigation of large and challenging membrane protein systems of pharmaceutical importance.

“With this work, we achieve a breakthrough for future NMR experiments of membrane proteins that always suffered from their high complexity. It can be envisioned that only the functionally relevant part of a membrane protein can be visualized to simplify the experiments even more. Such an approach will speed up the analysis of membrane protein structures and their interaction with drug molecules by NMR”, Prof. Hagn says.

Original publication

Daniilidis et al. (2024): Efficient Segmental Isotope Labeling of Integral Membrane Proteins for High-Resolution NMR Studies. Journal of the American Chemical Society. DOI: 10.1021/jacs.4c03294