Chaperonin-mediated protein folding at the surface of groEL through a'molten globule'-like intermediate
J Martin, T Langer, R Boteva, A Schramel, AL Horwich… - Nature, 1991 - nature.com
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.
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.
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.
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