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A protein that aids the assembly and folding of other protein molecules in living cells.
- ‘The best studied chaperone is the bacterial chaperonin, GroEL, a large protein shaped like a double ring with dyad symmetry under certain conditions.’
- ‘The biogenesis of microtubules in the cell comprises a series of complex steps, including protein-folding reactions catalyzed by chaperonins.’
- ‘In addition to folding new proteins, chaperonins also re-fold old proteins which have somehow gotten twisted out of shape.’
- ‘Further investigation, especially into the mechanical properties of misfolded proteins, is essential to clarify the functional mechanics of the chaperonin.’
- ‘However, not all complexes are so constrained, as illustrated by the evolution of the archael thermosome - yet another chaperonin composed of multiple rings of subunits.’
Late 20th century: from chaperone + -in.
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