The substrate binding domain of DnaK facilitates slow protein refolding

摘要: We examined the effects of a fragment substrate binding domain DnaK on protein refolding from chemically denatured states. The DnaK384-638, containing full-length domain, tightly binds to unfolded in solution. DnaK384-638 reactivation β-galactosidase and luciferase were at low concentration temperature, conditions which folding is significantly slow (several days) but yield higher than those ordinary conditions. In presence maximum active was improved 45% 65% after 48-h reaction. Spectroscopic experiments showed that bound partially structured monomers consequently suppressed aggregation. accelerated attain equilibrium 8 h. On other hand, DnaK386-561, has no affinity for substrate, had chaperone activity these proteins. These results indicate facilitates refolding.