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.
02/2022 How can aromatic residues undergo ring flipping in the core of a protein despite engaging in multiple stabilizing interactions to maintain protein fold? Read our new publication in Nature where we reveal the structural changes associated with ring flipping of a core tyrosine. Work led by postdoc Laura Mariño in collaboration with the Palencia group.
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.
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