A part of my research focuses on slow dynamics in proteins especially in relation to protein misfolding and aggregation. A major unresolved question in these processes is the roles of intermediates and how the structure and thermodynamic properties of these states relate to protein aggregation and fibrillation. These questions are addressed by a number of biophysical techniques including NMR spectroscopy, optical spectroscopy and light scattering techniques as well as protein engeneering. A number of proteins are studied, both proteins related to protein misfolding diseases and proteins that are pure model systems for protein unfolding and fibrillation.
An other line of research aims at understanding enzyme function and characterize the structure and thermodynamics the different states of both enzyme and substrate/product during catalysis. In this work NMR spectroscopy is the major experimental technique.
I am leading a FTP-funded project entitled “Functional Protein Dynamics” with Novozymes A/S and Lindorff-Larsen. I am also involved in the projects “Improving Carbohydrate Binding Properties of Cellulases” together with Novozymes A/S and the project “Understanding Mab stability” with Symphogen A/S. Together with Qunxin She (Biology, UCPH) I am involved in the FTP-funded project “Hot modifications” where a new stabilising post-translational modification in archaea has been discovered. I also collaborate with Jeppe T. Pedersen (Pharmacy, UCPH), Lars Hemmingsen (Chemistry, UCPH) and Peter Thulstrup, (Chemistry, UCPH) on understanding how metal-ions influences protein fibrillation and a project with Ulrik Gether (Neuropharm, UCPH) on “Structure and membrane interactions of the scaffolding protein PICK1”. Finally, I collaborate with Birthe B. Kragelund (Biology, UCPH) on several applications of NMR spectroscopy to address structure/dynamics relationships in proteins.
University of Copenhagen
Ole Maaloes Vej 5, room 3-0-39
DK-2200 Copenhagen N