Biomembrane force probe investigation of RNA dissociation.
Biomembrane force probe investigation of RNA dissociation.
复制标题
RNA 解离的生物膜力探针研究。
DOI：
10.1007/s00249-010-0642-7
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Brampton C
中科院分区：
文献类型：
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作者：
Brampton C
通过使用动态力光谱学的生物分子相互作用的能量途径的调查是有限的加载速率的范围内访问一个单一的技术。在本文讨论的工作中，这一范围已被扩展为以前研究的系统，通过使用生物膜力探针（BFP）。这项工作建立在我们以前的单分子原子力显微镜（AFM）研究的一个凸起的基序含有RNA复合物的解离。在高加载速率下观察到的具有和不具有中心三碱基对凸起的12碱基对复合物的解离之间的差异在低速率下未观察到。这表明，这两个物种共享一个类似的外部障碍解离，包括凸起基序创建一个额外的障碍，在距离更接近结合态。在不同缓冲液环境中进行的实验产生了类似的结果。结合之前的研究，这些结果表明，解离的共同外部障碍是由于螺旋末端的重排和磨损。
Investigations into the energy pathways of biomolecular interactions by use of dynamic force spectroscopy are limited by the range of loading rates accessible with a single technique. In the work discussed in this paper, this range has been extended for a previously studied system by using the biomembrane force probe (BFP). This work builds on our previous single-molecule atomic force microscopy (AFM) study of the dissociation of a bulge-motif-containing RNA complex. The disparity observed, at high loading rates, between the dissociation of a 12-base pair complex with and without a central three-base pair bulge was not observed at low rates. This suggests that the two species share a similar outer barrier to dissociation and that inclusion of the bulge motif creates an additional barrier at a distance closer to the bound state. Experiments performed in different buffer environments yielded similar results. The results, when combined with those of previous studies, suggest that the shared outer barrier to dissociation is that due to a rearrangement and fraying of the ends of the helix.