Accelerated Molecular Dynamics Simulations of Protein Folding

Folding of four fast‐folding proteins, including chignolin, Trp‐cage, villin headpiece, and WW domain, was simulated via accelerated molecular dynamics (aMD). Free energy profiles calculated through improved reweighting of the aMD simulations using cumulant expansion to the second‐order are in good agreement with those obtained from long‐timescale conventional molecular dynamics simulations. This work demonstrates the enhanced sampling power of aMD on protein folding and will provide basic references in using aMD for further studies.