Definition of chaperonin in English:
chaperonin
nounˌʃapəˈrəʊnɪnˌSHapəˈrōnən
Biochemistry A protein that aids the assembly and folding of other protein molecules in living cells.
Example sentencesExamples
- The best studied chaperone is the bacterial chaperonin, GroEL, a large protein shaped like a double ring with dyad symmetry under certain conditions.
- In addition to folding new proteins, chaperonins also re-fold old proteins which have somehow gotten twisted out of shape.
- The biogenesis of microtubules in the cell comprises a series of complex steps, including protein-folding reactions catalyzed by chaperonins.
- 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.
- Further investigation, especially into the mechanical properties of misfolded proteins, is essential to clarify the functional mechanics of the chaperonin.
Origin
1990s: from chaperone + -in.