نتایج جستجو برای: rna inverse folding
تعداد نتایج: 366102 فیلتر نتایج به سال:
Functional and structural inter-relationships of RNA and proteins in the execution and control of biological processes such as RNA processing, RNA splicing, and translation are increasingly apparent. In this minireview, I present an RNA chaperone hypothesis, which fosters the view that constraints imposed by fundamental problems in the folding of RNA have profoundly influenced the nature of RNA...
While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated by interaction with RNA. When an RNA-binding module is placed at the N-terminus of aggregation-prone target proteins, this module, upon bindin...
Before the discovery of catalytic RNA, tRNA molecules were the most studied RNA molecules for understanding RNA folding. Afterwards, group I introns, because of their stability and the fact that structural folding could be monitored by following their catalytic activity, became the molecule of choice for studying RNA architecture and folding. A major advantage of group I introns for studying th...
RNAomics, analogous to proteomics, concerns aspects of the secondary and tertiary structure, folding pathway, kinetics, comparison, function and regulation of all RNA in a living organism. Given recently discovered roles played by micro RNA, small interfering RNA, riboswitches, ribozymes, etc., it is important to gain insight into the folding process of RNA sequences. We describe the web server...
Ion-mediated electrostatic interactions play an important role in RNA folding stability. For a RNA in a solution with higher Mg(2+) ion concentration, more counterions in the solution can bind to the RNA, causing a strong many-body coupling between the bound ions. The many-body effect can change the effective potential of mean force between the tightly bound ions. This effect tends to dampen io...
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