Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
The original experiments reconstituting GroEL–GroES-mediated protein folding were carried out under ‘‘nonpermissive’’ conditions, where the chaperonin system was absolutely required and substrate proteins could not achieve the native state if diluted directly from denaturant into solution. Under ‘‘permissive’’ conditions, however, employing lower substrate concentration and lower temperature, some substrate proteins can be refolded
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