Overview of Research Interests
We are interested in structure, function and dynamics of two classes of proteins, membrane proteins, in particular receptors with function in signal transduction, and natively unfolded proteins and protein domains, with the following three focus areas:
Focus areas I & II: Mechanisms of folding and signaling function by membrane receptors.
Our research on membrane proteins focuses on the mechanisms of (I) folding and (II) activation-induced conformational changes: How can we explain diseases caused by membrane protein misfolding? Can we modulate membrane protein (mis)folding? What determines the folding, structure and stability of membrane proteins and how are these different from soluble proteins? How does folding relate to function, in particular during signaling by membrane receptors? What is the molecular nature of conformational changes induced by allosteric modulators and are these different from those induced by competitive drugs?
Focus area III: Natively unfolded states.
For natively unfolded proteins and protein domains, we are particularly interested in analyzing the functions of the natively unfolded states, their evolutionary conservation and ability to shift the conformational ensemble to more folded states.
We study the following systems:
Focus Areas I & II: Mechanisms of folding and signaling function by membrane receptors
For further information on some of these systems click here. For a general review of G protein coupled receptor research click here. Pls. note that pdf file of references cannot be accessed without password for copyright reasons.
Focus Area III: Natively unfolded states
- Cytoplasmic domain of growth hormone receptor
- Glutamic acid rich proteins
- Cytoplasmic tail of G protein coupled receptor rhodopsin
- Cytoplasmic domain of transducer
We use an interdisciplinary combination of computational and experimental, in particular biochemical and biophysical, approaches: