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Unusual Dynamics and pKa Shift at the Active Site of a Lead-Dependent Ribozyme

机译:铅依赖性核酶活性部位的异常动力学和pKa位移

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摘要

Heteronuclear NMR spectroscopy has been used to probe the structure and dynamics of a lead-dependent ribozyme known as the leadzyme. The pKa's for all adenine bases in the leadzyme were measured and vary from <3.1 to 6.5. The adenines with the lowest pKa's are involved in Watson-Crick base pairs, and the adenine with the highest pKa is thought to form an AH~+ -C wobble base pair at the active site of the leadzyme.
机译:核磁共振波谱已用于探测称为铅酶的铅依赖性核酶的结构和动力学。测量了铅酶中所有腺嘌呤碱基的pKa,范围从<3.1到6.5。 Watson-Crick碱基对涉及pKa最低的腺嘌呤,pKa最高的腺嘌呤被认为在铅酶的活性位点形成AH〜+ -C摆动碱基对。

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