Elucidation of mechanism for conformational change and protein folding of the group 2 chaperonin

为了阐明2组伴侣蛋白（CPN）的详细构象变化和蛋白质折叠机制，我们采用停流荧光法、停流小角x射线散射法和衍射x射线跟踪法对构象变化进行了动力学研究。结果表明，构象变化是双相的，后者包括环的旋转运动。此外，我们利用圆形排列连接突变体构建并表征了由野生型环和突变型环组成的不对称环复合物。研究结果对CPN的环内通信有了新的认识。

To elucidate detailed conformational change and protein folding mechanism of the group 2 chaperonin(CPN), we have performed kinetic studies of conformational change by stopped-flow fluorometry, stopped-flow small angle X-ray scattering and Diffracted X-ray Tracking. The results have shown that the conformational change is biphasic and the latter includes the rotational motion of the ring. In addition, we constructed and characterize asymmetric ring complex that consists of a wild-type ring and a mutant ring by using circular permutated connected mutants. The results gave an insight on the inter ring communication of CPN.