Roberta Pierattelli

This study characterizes the conformational dynamics and phosphorylation-dependent changes in the SF3B1 N-terminal domain using a combination of biophysical and computational methods.

This study designs metamorphic proteins that switch between multiple conformations and shows how mutations can shift their conformational equilibrium.

The paper shows a small molecule selectively targets an oligomeric form of a protein with an intrinsically disordered region, altering its interaction network and condensation properties.

The paper analyzes human spliceosome proteins to show that many contain over 40% disordered residues, driven by compositional bias and linked to post-translational modifications and cancer mutations.