Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate.

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

Nature

journal_title

Nature

authors

Martin J,Langer T,Boteva R,Schramel A,Horwich AL,Hartl FU

doi

10.1038/352036a0

subject

Has Abstract

pub_date

1991-07-04 00:00:00

pages

36-42

issue

6330

eissn

0028-0836

issn

1476-4687

journal_volume

352

pub_type

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