Pierre Tufféry

This paper introduces SST2, a new enhanced sampling method for molecular dynamics simulations that improves efficiency for large biomolecular systems by selectively scaling interactions within and around the molecule.

The paper explores cyclic peptide conformations using multiple molecular dynamics protocols and force fields, finding that combining implicit solvent simulations improves native structure prediction.

The paper identifies conserved protein motifs in KAKU4 and related nucleoporins that mediate nucleoskeleton attachment to nuclear pores in plants.

This study improves peptide structure prediction by incorporating pH and salt effects into a coarse-grained model, showing better performance for poly-charged peptides and sequences without homologs.

The paper introduces a framework for rational head-to-tail peptide cyclization using protein structure data, demonstrating improved conformation prediction and successful application to Nrf2 and urotensin II peptides.

The paper identifies peptides that disrupt the LRRK2/PP1 interaction and validates their in vitro and in vivo activity.