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.
01/2022 Our study on the interaction of the SARS-CoV-2 nucleoprotein with its viral partner nsp3a is out in Science Advances. Work in collaboration with the Blackledge team.
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.
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