Conformational Distribution and Ultrafast Base Dynamics of Leadzyme
Conformational Distribution and Ultrafast Base Dynamics of Leadzyme
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DOI：
10.1021/bi900256q
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发表时间：
2009-05-12
期刊：
影响因子：
2.9
通讯作者：
Xia, Tianbing
中科院分区：
文献类型：
--
作者：
Kadakkuzha, Beena M.;Zhao, Liang;Xia, Tianbing
核酶的动力学性质是阐明其结构-动力学-功能关系的一个重大挑战。在这里，使用飞秒时间分辨光谱和其他生物物理工具，我们证明了leadzyme的活性位点不具有独特的结构，而是样品的构象，经历皮秒结构变化的合奏。各种碱基修饰对催化作用具有深刻的上下文依赖性影响。
The dynamic nature of ribozymes represents a significant challenge in elucidating their structure-dynamics-function relationship. Here, using femtosecond time-resolved spectroscopy and other biophysical tools, we demonstrate that the active site of leadzyme does not have a unique structure, but rather samples an ensemble of conformations that undergo picosecond structural changes. Various base modifications have a profound context-dependent impact on the catalysis.