MOLECULAR DYNAMIC SIMULATION OF CHAPERONIN-MEDIATED PROTEIN-FOLDING

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