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NMR Spectroscopy

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Vincent Truffault

+49 7071 601-1359


The functions of proteins rely on their structures and the structural changes they can undergo. Structural biology hence provides unique insights into biomolecular function and thereby into cellular processes. Furthermore, the knowledge of protein structures is an invaluable starting point in the development of drugs to treat human disease. Nuclear magnetic resonance (NMR) spectroscopy is the only method available to study biomolecular structure and dynamics with atomic resolution in solution. NMR provides information on the three-dimensional fold of proteins and the way proteins interact with other biomolecules. Finally, NMR spectroscopy gives insights into how protein complexes move and change conformation, aspects that are important for many enzymatic reactions. The information gained by NMR about biomolecular structure, interactions and dynamics allows us to understand how proteins are able to perform specific tasks in the cell.
NMR spectroscopy exploits a physical property called “spin” that certain atoms (e.g. 1H, 13C, and 15N) possess. If a protein is placed in a strong magnetic field, these atoms resonate at a “spin-frequency” that is unique to each atom. Since the resonance frequency depends on the chemical environment of the atom, it provides information about the atomic structure of the protein. The Max Planck Institute for Developmental Biology installed two state-of-the-art NMR magnets (600 and 800 MHz spectrometers) in the summer of 2008 that are currently in full operation. Both machines are used by four research groups (see below) and have already enabled us to gain exciting novel insights into biomolecular function.

Selected Publications


600 MHz Bruker Avance-III
800 MHz Bruker Avance-III