Chen

Chun

Gallagher

Leland Mayne

Mayne

S. Walter Englander

Sirur

Xiang Ye

Zhong-yuan Kan

Significance
          The GroEL/ES chaperonin is known to prevent protein aggregation during folding by passive containment within the central cavity. The possible role of more active intervention is controversial. The HX MS method documents an organized hydrophobically stabilized folding preintermediate in the collapsed ensemble of maltose binding protein. A mutational defect destabilizes the preintermediate and greatly slows folding of the subsequent on-pathway H-bonded intermediate. GroEL encapsulation alone, without ATP and substrate protein cycling, restabilizes the preintermediate and restores fast folding. The mechanism appears to depend on forceful compression during confinement. More generally, these results suggest that GroEL can repair different folding defects in different ways.</jats:p

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Proceedings of the National Academy of Sciences

Folding of maltose binding protein outside of and in GroEL

Folding of maltose binding protein outside of and in GroEL

Abstract

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