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NMR spectroscopy to unravel biomolecular mechanisms

Proteins and their interactions play key roles in many biological functions. We use nuclear magnetic resonance (NMR) spectroscopy to resolve structure and function of proteins at atomic resolution and thus unravel their molecular mechanisms.

Proteins are responsible for a wide range of essential biological functions, including signal transduction, catalysis, cellular homeostasis, metabolism and membrane transport. We characterize the underlying molecular processes at atomic resolution by solution NMR spectroscopy and related techniques. Part of our activities is the development of new and improved NMR techniques for challenging biomacromolecules including membrane proteins.

Principles of chaperone function 
In all kingdoms of life, molecular chaperones overtake key roles in cellular proteostasis including interaction and transport of unfolded polypeptide chains. We employ high-resolution NMR spectroscopy to determine conformation and dynamics of large chaperone–client complexes including membrane-protein clients at the atomic level. These help us to understand in detail which biophysical laws govern chaperone function, including how chaperones recognize client proteins, and how clients are transferred between chaperones.

Outer membrane protein biogenesis and its role for novel antibiotics
Outer membrane proteins are transported by molecular chaperones to the outer membrane and then are folded and inserted into the membrane by the Bam complex. We are investigating the mechanisms of folding and insertion, both for the Bam-catalyzed and the uncatalyzed reaction. At the same time, BamA is a highly valuable target for the novel antibiotics OMPTA and darobactin. We are currently investigating their mode of action at atomic detail. 

Dynamic kinases and kinase interactions
Kinases govern central cellular functions, including signaling and the regulation of metabolism. We investigate how bacterial kinases are controlled by signaling molecules to undergo cell cycle-dependent switches and how the mammalian TOR protein complex interacts with its dynamic substrate proteins to result in well-coordinated activation of proteins. These interaction studies between flexible substrates and well-folded, gigantic kinase molecules benefit optimally from the power of solution NMR spectroscopy.

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