Protein dynamics and interactions by NMR spectroscopy
The Hansen Lab focuses on the study of protein dynamics using nuclear magnetic resonance (NMR) techniques. NMR method development is a major part of our research, as well as the combination of NMR with computational tools. We are particularly interested in the dynamics, function, and regulations of human histone deacetylases (HDACs) and domains of the von Willebrand Factor (vWF).
Selected publications
Measurement of 15N longitudinal relaxation rates in 15NH4+ spin systems to characterise rotational correlation times and chemical exchange
Hansen, D.F.
Journal of Magnetic Resonance (2017) 279:91-98
Journal of Magnetic Resonance (2017) 279:91-98
Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction
Zeymer, C., Werbeck, N.D., Zimmermann, S., Reinstein, J., Hansen, D.F.
Angewandte Chemie International Edition (2016) 55 (38):11533–11537
Angewandte Chemie International Edition (2016) 55 (38):11533–11537
Solution structure of the major factor VIII binding region on von Willebrand factor
Shiltagh, N., Kirkpatrick, J., Cabrita, L.D., McKinnon, T.A.J., Thalassinos, K., Tuddenham, E.G.D., Hansen, D.F.
Blood (2014) 123 (26):4143-4151
Blood (2014) 123 (26):4143-4151