Bruno de Paula Oliveira Santos

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.

The paper presents a workflow combining CCPNMR2.4 and ARIA2.3 to handle N-terminal acetylation and C-terminal amidation in protein structure calculation, showing no significant difference from existing methods.