Titlebook: Non-Protein Coding RNAs; Nils G. Walter (Associate Professor of Chemistry), Book 2009 Springer-Verlag Berlin Heidelberg 2009 Einzelmolekül

LUMEN

Beyond Crystallography: Investigating the Conformational Dynamics of the Purine Riboswitch,ir ability to specifically bind metabolites. The purine riboswitch ligand-binding domain has emerged as an important model system for investigating the relationship between RNA structure and function. Directed by NMR and crystallographically generated structures of this RNA, a variety of biophysical

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Ligand Binding and Conformational Changes in the Purine-Binding Riboswitch Aptamer Domains, riboswitches bind different purine ligands by forming both canonical Watson—Crick and non-canonical intermolecular base pairs, involving a variety of hydrogen bonds between the riboswitch aptamer domain and the purine ligand. Here, we summarize work on the ligand binding modes of both purine-bindin

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,The RNA–Protein Complexes of , Hfq: Form and Function,base-pairing between mRNAs and ncRNAs leading to translational activation, translational repression and/or degradation of mRNAs — the bacterial analog of the RNA interference pathway. Hfq is the bacterial homolog of the Sm and Lsm proteins and has a similar doughnut-shaped structure. This review sum

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Genome

ODIUM

Constrain

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Structure and Gene-Silencing Mechanisms of Small Noncoding RNAs,cing phenomenon, RNA interference (RNAi), is triggered in a sequence-specific manner by endogenously produced or exogenously introduced small doubled-stranded RNAs. As knowledge of the structure and function of the RNAi machinery has expanded, this phenomenon has become a powerful tool for biochemic

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Melanoma

Ligand Binding and Conformational Changes in the Purine-Binding Riboswitch Aptamer Domains, in the free form. A more stable helix II in the guanine riboswitch leads to a preformed loop—loop interaction in its free form. In contrast, a less stable helix II in the adenine riboswitch results in a lack of this loop—loop interaction in the absence of ligand and divalent cations.