Proteins function by interacting with other molecules. In some cases, the biological function is the interaction itself, while the biological function in other cases is to catalyze some change in the bound molecule. In both cases, it is fundamental that the protein can adapt structurally to the molecule it interacts with. Consequently, proteins are dynamic and constantly change their conformations.
In the Teilum group at the Structural Biology and NMR Laboratory at the Linderstøm-Lang Centre for Protein Science, Department of Biology we use NMR spectroscopy in combination with other biophysical techniques to understand how conformational dynamics is associated with protein function.
Currently, we have available projects at the B.Sc. and M.Sc. levels within the following headlines:
- Ligand induced conformational changes in a fold switching protein.
- Dynamics and assembly of endogenous retroviral Gag proteins.
- Hydrogen exchange as a tool to measure transient structure formation in disordered proteins.
For more specific details, contact Kaare Teilum (email@example.com) for an informal meeting.
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Sektion for Biomolekylære Videnskaber, Proteinkemi, Biofysik, Protein, Biokemi, Proteinoprensning, Spektroskopi