RNA Cold Denaturation

超出了3个预留空间。RNA在生物化学的许多方面起着核心作用。为了实现这些细胞功能，RNA保持其复杂的二级、三级和四级结构至关重要。此外，越来越明显的是，RNA容易在两个或更多个稳定（或假稳定）结构之间相互转化，作为其正常生物功能的一部分。这些重排可以参与核酶活性的控制，如在对接的情况下，或通过在5 '-或3'-UTR中形成替代结构的mRNA的翻译控制。该项目围绕理解在某些RNA中观察到的结构变化的热力学基础。我们关注的一种结构变化是RNA在低温下展开的冷变性过程。对这些过程特别重要的是在折叠时热容（Acp）的变化，这是以前认为可以忽略不计的性质，但现在显示在某些情况下是重要的。锤头状核酶的冷变性是迄今为止研究得最好的，也是第一个具体目标的焦点。然后将冷变性的热力学与由高温和离液剂诱导的变性进行比较。冷变性的普遍性将作为具体目标2的一部分进行探讨，以及冷变性和冷休克反应中涉及的核糖调节过程之间的关系。一个小的非编码RNA从E.一种叫做DsrA的螺旋参与调节这个过程，我们正在探索这种RNA的结构变化，以及这些结构变化如何影响它与蛋白质（Hfq）和其他RNA形成的复合物。该提案的第三个主要目标是研究AH和ACP在核酸折叠中的潜在性质，并了解金属水合/脱水反应对RNA三级结构形成的总体能量学的热力学贡献。性能现场=

EXCEED THE SPACE 3ROVIDED. RNA plays a central role in many aspects of biochemistry. To carry out these cellular functions, it is critical that RNAs maintain their complex secondary, tertiary and quaternary structures. Furthermore, it is becoming evident that RNAs readily interconvert between two or more stable (or pseudo-stable) structures as part of their normal biological function. These rearrangements can be involved in control of ribozyme activity as in the case of docking, or translational control of an mRNA through formation of alternative structures in the 5'- or 3'-UTRs. This project revolves around understanding the thermodynamic basis for the structural changes observed in certain RNAs. One type of structural change we focus on is the process of cold denaturation where RNAs unfold at low temperature. Of particular importance to these processes is the change in heat capacity (ACp) upon folding, a property previously believed to be negligible but now shown to be significant in certain cases. The cold denaturation of the hammerhead ribozyme is the best studied to date and the focus of the first specific aim. The thermodynamics to cold denaturation will then be compared to denaturation induced by high temperature and chaotropic agents. The generality of cold denaturation will be probed as part of specific aim 2 as well as the relationship between cold denaturation and riboregulation processes involved in the cold shock response. A small non-coding RNA from E. coil called DsrA is involved in regulating this process are we are probing the structural changes of this RNA and how these structural changes affect the complexes it makes with proteins (Hfq) and other RNAs. The 3rd major goal of this proposal is to look a the underlying nature of AH and ACp in nucleic acid folding and understand the thermodynamic contribution of metal hydration/dehydration reactions on the overall energetics of tertiary structure formation of RNAs. PERFORMANCE SITE ========================================Section End===========================================