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Chaperonin |
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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 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. Want to thank TFD for its existence? Tell a friend about us, add a link to this page, add the site to iGoogle, or visit the webmaster's page for free fun content. |
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No references found | XToll, a recombinant chaperonin 10 as an anti-inflammatory immunomodulator. suis were used in this study: cpn60, dpr, recA, aroA, thrA, gki, and mutS coding for a 60-kDa chaperonin, a putative peroxide resistance protein, a homologous recombination factor, a 5-enolpyruvylshikimate 3-phosphate synthase, an aspartokinase/homoserine dehydrogenase, a glucose kinase, and a DNA mismatch repair enzyme, respectively (8). 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. |
Chaperonin |
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