释义 |
chaperonin
chap·er·o·nin C5251250 (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. [chaperon(e) + -in.]chaperonin
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 (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 |