Definition of chaperonin in English:

chaperonin

nounˌʃapəˈrəʊnɪnˌSHapəˈrōnən

Biochemistry

A protein that aids the assembly and folding of other protein molecules in living cells.
〔生化〕陪伴蛋白
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.

Definition of chaperonin in US English:

chaperonin

nounˌSHapəˈrōnən

Biochemistry

A protein that aids the assembly and folding of other protein molecules in living cells.
〔生化〕陪伴蛋白
Example sentencesExamples
- 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.
- 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.

Origin

1990s: from chaperone + -in.

单词	chaperonin
释义	Definition of chaperonin in English: chaperonin nounˌʃapəˈrəʊnɪnˌSHapəˈrōnən Biochemistry A protein that aids the assembly and folding of other protein molecules in living cells. 〔生化〕陪伴蛋白 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. Definition of chaperonin in US English: chaperonin nounˌSHapəˈrōnən Biochemistry A protein that aids the assembly and folding of other protein molecules in living cells. 〔生化〕陪伴蛋白 Example sentencesExamples 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. 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. Origin 1990s: from chaperone + -in.
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