chaperonin

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chaperonin

(shap-ĕr-ō'nin),
A molecular complex composed of multiple heat shock protein subunits that assemble into double ring structures. Chaperonins function within the cytoplasm to refold damaged proteins.
See also: heat shock proteins.
[chaperon + -in]

chaperonin

/chap·er·o·nin/ (shap″er-o´nin) any of various heat shock proteins that act as molecular chaperones in bacteria, plasmids, mitochondria, and eukaryotic cyotsol.

chaperonin

(shăp′ə-rō′nĭn)
n.
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.
Any of a group of 60 kD cytosolic chaperone proteins—e.g., heat shock protein 60, hsp60, GroEL—found in prokaryotes, the equivalent of the eukaryotic hsp60, mitochondria and plastids; chaparonins use energy from ATP hydrolysis to maintain proteins in the necessary folded configuration for proper function, thus having ‘foldase’ activity; other postulated roles for chaperonins include protein transport, oligomer assembly, DNA replication, mRNA turnover, and protection of the cell from various stresses; some chaperonins have auto-foldase activities

chaperonin

a class of chaperone proteins.
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References in periodicals archive ?
These portals extend deep into the slice and probably provide the chaperonin with a place for processing energy-transfer molecules called ATP, Sigler notes.
Eight induced proteins were identified as DnaK protein, fabG4 protein, DNA-binding protein, hypothetical protein, two 14 kDa antigen and two 10 kDa chaperonin.
Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures.
Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant.
In an effort to examine the location and the conformational properties of a polypeptide chain substrate chaperonin complexes, SANS experiments with contrast variation were undertaken at the NCNR by CARB (Center for Advanced Research in Biotechnology) and NCNR scientists, using a 86 % deuterated nonnative.
Although scientists have known for almost a decade that chaperonins aid proteins in folding, the precise mechanism of this process has remained murky.
Scientists had already generated precise pictures of chaperonins before and after these molecular guardians assisted in protein folding, but they lacked detailed images of what happens in between.
The study provides a snapshot that shows how and why chaperonins stimulate folding," says team member Arthur L.
The researchers used information from their new picture to design experiments that explore how chaperonins exploit ATP, the small, energy-packed molecule that cells use to drive reactions.
To discourage the wayward clumping behavior, chaperonins sequester young proteins.