Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

(2009) D. K. Clare et al.   NATURE

Probing Protein-Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy

(2008) Frank Hillger et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

(2008) Shruti Sharma et al.   CELL

Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL

(2008) Tatsuya Nojima et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side

(2008) Yali Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Triggering Protein Folding within the GroEL-GroES Complex

(2008) Damian Madan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Concerted Release of Substrate Domains from GroEL by ATP Is Demonstrated with FRET

(2008) Niv Papo et al.   JOURNAL OF MOLECULAR BIOLOGY

GroEL stimulates protein folding through forced unfolding

(2008) Zong Lin et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state

(2008) E. Chapman et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

(2008) A. C. Apetri et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA