Our research team focuses on elucidating the role of intrinsically disordered proteins (IDPs) in biology. In particular, we are interested in the mitogen-activated protein kinase (MAPK) cell signaling pathways and how intrinsically disordered scaffold proteins regulate signaling specificity and MAPK activity. We use NMR spectroscopy combined with X-ray crystallography and biophysics to study these dynamic assemblies at atomic resolution.
08/2021 How can IDPs fold into two different conformations upon binding to different protein targets while keeping the same binding affinity? The key is enthalpy-entropy compensation. Read our new publication here.
10/2020 Lenette Frøsig Kjær joins the team as a Ph.D. student
08/2020 Our recent paper describing the molecular mechanisms underlying the switch from the lysogenic to the lytic state in a temperate bacteriophage is out in PNAS. A nice collaboration with the groups of Prof. Leila Lo Leggio (University of Copenhagen) and Dr. Mogens Kilstrup (Technical University of Denmark).
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