Abstract:
:Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg-ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.
journal_name
Naturejournal_title
Natureauthors
Martin J,Langer T,Boteva R,Schramel A,Horwich AL,Hartl FUdoi
10.1038/352036a0subject
Has Abstractpub_date
1991-07-04 00:00:00pages
36-42issue
6330eissn
0028-0836issn
1476-4687journal_volume
352pub_type
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