Functional and kinetic analysis of the inter-domain communication network of the chaperonin GroEL

采用循环置换和停流荧光分析相结合的方法，探讨了GroEL促进蛋白质折叠的分子机制与GroEL蛋白独特的三域亚基结构之间的关系。通过对多个循环排列的GroEL变体的分析，我们成功地将特定的、结构域相关的构象变化与伴侣机制的一个重要功能方面关联起来。此外，我们的结果促使对GroEL促进折叠的传统机制进行了重新评估。

A combination of circular permutation and stopped-flow fluorescence analysis was utilized to probe the relationship between the molecular mechanism of GroEL-facilitated protein folding and the unique three-domain subunit structure of the GroEL protein. Through analysis of multiple circularly permuted GroEL variants, we succeeded in correlating a specific, domain-dependent conformational change to an important functional aspect of the chaperonin mechanism. Additionally, our results prompt a reevaluation of the conventional mechanism of GroEL-facilitated folding.