Review of ’Protein folding guides disulfide bond formation’

Abstract

The mechanism of how protein folding drives disulfide bond formation is poor understood and the methods implemented on molecular dynamics software usually do not cover the problem of disulfide bond. Meng, using coarse-grained molecular simulation with disulfide bonds stabilized a harmonic potential, created a novel way to mimic the formation and rupture of disulfide bonds. By implementing his method to the bovine pancreatic trypsin inhibitor, the folding mechanism of this protein are resolved and as anticipated, the disulfide bonds do have important effect in folding process