ATP-Induced Shape Change in a Model Protein Complexed in Chaperonins

摘要

The role of molecular chaperones in mediating and controlling intrucel liilar, as well as in vitro protein folding, has broad implications for biotechnology. There is now considerable insight into the possible mechanisms whereby chaperone proteins recognize. stabilize, and release unfolded polypeptide chains in a manner shcreby (hey are able IA) productively refold. However. there arc a number of iniportant. fundamental gaps in the understanding of chaperone action, which remain to he resolved. Among the growing list of chaperone families are the chaperonins GruEL (EL) and GroES (ES). which have been intensively studied. Knowledge of how mislolded protein substrates physically interact with EL should provide vital clues necessary to unravel the process h which EL mediates their proper folding. The ultimate goal is to deteniinc the mechanism by which EL transforms its substrate proteins and then releases them in a form able to refold to their native conformation.