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Membrane protein structure and function

Membrane proteins act as the central interface between environment and cellular response. Due to practical reasons high-resolution insights into membrane protein structure and function is often obtained by replacing the native lipid bilayer environment with detergent molecules.

We are using two approaches to circumvent intrinsic disadvantages of detergent systems:
1. Solid-state NMR in a near native environment (i.e. proteoliposomes)
2. Solution-state NMR in detergent free environments (e.g. lipid-bilayer nanodiscs)

We aim to identify and apply the most suitable technique and membrane mimetic for a given system.
Therefor we are using on the one hand well-established test proteins such as bacteriorhodopsin to explore feasibilities and limitations of promising non-conventional tools such as nanodiscs and amphipathic polymers. On the other hand we make use of the obtained information to advance the characterization of more challenging and pharmacologically relevant membrane proteins. For the latter we are in particular interested in understanding the molecular mechanism involved in hormone-receptor interactions.

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