Molecular mechanism of a thioredoxin-like protein investigated by MD simulations

by Daniele Narzi (Universitat Erlangen-Nornberg (Germany))

Monday 18 Jul 2011, 16:00 → 18:00 Europe/Rome

Aula Conversi (Dip. di Fisica - Edificio G. Marconi)

Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in proteins. Here, combining Poisson-Boltzmann-based protonation-state calculations and Molecular Dynamics simulations, we investigate the catalytic mechanism of the Trx-like protein DsbL. We observed several correlated transitions in the protonation states of a buried active-site cysteine and a neighboring lysine. Based on our findings a consistent catalytic mechanism for DsbL is presented.