Research in the Structural Biology and NMR Laboratory

Click on the names to learn more about the research in the individual laboratories.

• Birthe B. Kragelund

  Signal transduction is often conveyed through protein-protein interactions via specific atomic interactions. In the cell there are a multitude of different types of interactions between proteins and their partner molecules. The understanding of the interactions at the molecular level is key to understanding and controlling 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.

• Kresten Lindorff-Larsen

  The primary tools used in our research are computational methods that we use to study the structure and dynamics of proteins. A particular focus is methods that combine experimental data from NMR spectroscopy with molecular simulations. In one set of studies we combine experiments and simulations to provide a detailed structural interpretation of the experimental data. In another methods to predict what mutations are likely to occur and give rise to drug resistance and what possible mutations giving rise to drug resistance would actually render the enzyme inactive.

• Kaare Teilum

  Several examples have emerged of enzymes where slow conformational changes are of key importance for function. Our description of how flexibility in enzymes influences the catalytic activity is however sparse and not at a level where it can enable the optimization of enzyme function. Our strategy is to make a thorough characterization of the flexibility in enzymes using NMR spectroscopy, X-ray diffraction and computational methods and use the insights to interpret and rationalize the effects of point mutations on the flexibility, stability and catalysis of enzymes in general.