Luca Grisanti

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

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.

This study uses molecular dynamics to analyze the conformational behavior of the Amyloid β30-35 peptide in water, revealing its intrinsically disordered nature and the role of hydrogen bonds and hydrophobic interactions.