I lead one of three research groups at the Structural Biology and NMR Laboratory (SBiN-Lab) at the Department of Biology. The major expertise of the group is in protein interaction, structure and function relationships investigated by NMR spectroscopy as well as in biophysics. A hallmark is a strong collaborative base with biology, medicine, and industry.

I have significant experience with teaching and student supervision and allways have projects on hand. 

Protein-Protein Interactions - Understanding Functional Interactions from a Structural Platform

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 Center. Read more about REPIN here.

Collaborations

Our research is strongly dependent on collaborations with cell biology and biology laboratories as well as with industry. At present, we collaborate closely with Dr. Vincent Goffin, INSERM, Paris France, Prof. Joseph Martial, and Dr. Ingrid Struman, Université de Liege, Belgium; Prof Antony Carr and Dr. Kostas Nestorastos, University of Sussex, England; Prof Ciro Cicconi, University of Modena, Italy; Dr. Med. Ole E. Sørensen, BMC, Lunds University, Dr. Paul Hansen, LIFE, University of Copenhagen, Dr. Egon Persson, Novo Nordisk A/S, Prof. Olaf Nielsen, Dr. Stine Falsig Pedersen, Dr. Karen Skriver, Dr. Kresten Lindorff-Larsen and Dr. Kaare Teilum, Department of Biology, University of Copenhagen.

RESEARCH INTERESTS AND KEY QUALIFICATIONS

Protein interaction principles, protein structure and function relationships, protein-receptor interactions and mechanisms of activation, membrane proteins, protein folding, intrinsically unfolded proteins, structure determination of larger protein systems by NMR spectroscopy, hormone action, anti-angiogenesis, amyloids.

• NMR spectroscopy and Optical spectroscopy
• Protein refolding and purification, protein chemistry
• Mechanism of protein-receptor activation - Protein-protein interactions

PROFESSIONAL CAREER

ADMINISTRATIVE AND ORGANISATION SKILLS

TEACHING ACTIVITIES

• Responsible teacher for the course Protein Science (3rd year courses).
• Teacher at the course Protein Chemistry and Enzymology (1st year course).
• Adviser for a total of 5 Ph. D. students and 23 master students.
• Graduated master students since 2003: 18
• Graduated Ph. D. students since 2005: 4