Molecular dynamic simulation of chaperonin-mediated protein folding

We use molecular dynamics methods to simulate chaperonin-mediated refolding of barnase. A "chaperonin" term is added to the force field in order to simulate the hydrophobic environment in the central cavity of the chaperonins. Two aspects of our simulation results are consistent with experiments: (1) The hydrophobic environment of the central cavity of the chaperonin is an advantageous condition for the refolding of the misfolded intermediates. (2) One cycle of binding and release is not enough for the successful folding. Chaperonin-assisted protein folding maybe a procedure of multiple cycles of binding and release from the chaperonin.