One facet of the complexity of life is the cascade of signaling caused by thousands of proteins transferring unambiguous signals that instantly will regulate production and activities in the cell at the molecular level. Signal transfer is often conveyed through protein-protein interactions via specific atomic interactions. In the cell there are a multitude of different types of interaction between proteins and their partner molecules. The understanding of the molecular details of these interactions is a key to steering of protein function. By application of NMR spectroscopy, x-ray crystallography, protein engineering and biophysical techniques we seek to map mechanisms of interactions involved in i.e. receptor activation, cell division, signal transduction, immune activation and protein degradation. We focus on

  • Membrane bound protein receptors
  • Intrinsically unfolded proteins
  • Anti-microbial peptides 

The interactions involving these protein classes are particularly important as they make possible either the transfer of signal across membranes or the transfer of information from an unstructured protein which is a profound challenge to the structure-function paradigm. All three classes of proteins recognize and interact with an equal or even bigger number of proteins of different sizes, structures and mechanisms of function. To understand how a biological active molecule selects and discriminates between different possible interaction partners as well as the principles behind these interactions are important questions in protein science and molecular biology of today.

We currently pursue our goals within the areas of membrane proteins and intrinsically unfolded proteins in the context of REPIN, a Novo Nordisk Foundation Challenge Centre. Read more about the centre here.