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Martin J, Langer T, Boteva R, et al. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 1991;352(6330):36-42doi: 10.1038/352036a0.
Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F. U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature, 352(6330), 36-42. https://doi.org/10.1038/352036a0
Martin, J, et al. "Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate." Nature vol. 352,6330 (1991): 36-42. doi: https://doi.org/10.1038/352036a0
Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 1991 Jul 04;352(6330):36-42. doi: 10.1038/352036a0. PMID: 1676490.
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Nature. 1991 Jul 04;352(6330):36-42. doi: 10.1038/352036a0.

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

Nature

J Martin, T Langer, R Boteva, A Schramel, A L Horwich, F U Hartl

Affiliations

  1. Institut für Physiologische Chemie Universität München, Germany.

PMID: 1676490 DOI: 10.1038/352036a0

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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