Interplay of structure and disorder in cochaperonin mobile loops (Q27733719)

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A Taher

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C Georgopoulos

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S M van der Vies

Proceedings of the National Academy of Sciences of the United States of America

4

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language of work or name

English

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publication date

15 October 1996

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published in

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volume

93

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issue

21

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page(s)

11622-7

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Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli

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The universally conserved GroE (Hsp60) chaperonins

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Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein

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Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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Binding of chaperonins.

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19 June 2018

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Characterization of a functionally important mobile domain of GroES.

27 November 2018

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

27 November 2018

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Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

27 November 2018

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Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

27 November 2018

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How chaperones tell wrong from right

27 November 2018

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12 December 2020

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

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12 December 2020

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

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12 December 2020

Identification of 1H resonances from the bait region of human alpha 2-macroglobulin and effects of proteases and methylamine

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12 December 2020

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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12 December 2020

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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12 December 2020

Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly

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12 December 2020