A remarkable structure of an 86 kDa substrate encapsulated in a single-ring GroEL/GroES chaperonin complex is revealed by cryo-electron microscopy in this issue of Structure (Chen et al., 2006). Surprisingly, the protein-folding chamber is 80% larger than that of the double-ring GroEL/ES structure
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coil have an essen...
AbstractThe chaperon in GroEL is a large, double-ring structure that, together with ATP and the coch...
The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of ...
AbstractGroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and ...
AbstractThe chaperonin GroEL binds nonnative proteins too large to fit inside the productive GroEL-G...
AbstractChaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by...
AbstractThe chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of...
SummaryThe chaperonin GroEL interacts with various proteins, leading them to adopt their correct con...
SummaryElectron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of Gr...
AbstractThe chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them a...
AbstractRecent studies of GroE-mediated protein folding indicate that substrate proteins are product...
SummaryThe chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actio...
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of su...
The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substr...
AbstractThe chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilita...
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coil have an essen...
AbstractThe chaperon in GroEL is a large, double-ring structure that, together with ATP and the coch...
The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of ...
AbstractGroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and ...
AbstractThe chaperonin GroEL binds nonnative proteins too large to fit inside the productive GroEL-G...
AbstractChaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by...
AbstractThe chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of...
SummaryThe chaperonin GroEL interacts with various proteins, leading them to adopt their correct con...
SummaryElectron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of Gr...
AbstractThe chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them a...
AbstractRecent studies of GroE-mediated protein folding indicate that substrate proteins are product...
SummaryThe chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actio...
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of su...
The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substr...
AbstractThe chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilita...
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coil have an essen...
AbstractThe chaperon in GroEL is a large, double-ring structure that, together with ATP and the coch...
The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of ...
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